Subtilisin variants having improved stability

ABSTRACT

Disclosed herein is one or more subtilisin variant, nucleic acid encoding same, and compositions and methods related to the production and use thereof, including one or more subtilisin variant that has improved stability compared to one or more reference subtilisin.

The present application claims priority to U.S. Provisional Application62/772,271, filed Nov. 28, 2018, the entirety of which is herebyincorporated by reference.

Disclosed herein is one or more subtilisin variant, and compositions andmethods related to the production and use thereof, including one or moresubtilisin variant that has improved stability and/or soil removalcompared to one or more reference subtilisin.

REFERENCE TO SEQUENCE LISTING SUBMITTED ELECTRONICALLY

The content of the sequence listing electronically submitted with theapplication as an ASCII text file (Name:20191120_NB41589PCT_ST25_SeqLst.txt; Size: 84 KB; Created: Nov. 20,2019) forms part of the application and is hereby incorporated herein byreference in its entirety.

BACKGROUND

A protease (also known as a proteinase) is an enzyme that has theability to break down other proteins. A protease has the ability toconduct proteolysis, by hydrolysis of peptide bonds that link aminoacids together in a peptide or polypeptide chain forming the protein.This activity of a protease as a protein-digesting enzyme is termed aproteolytic activity. Many well-known procedures exist for measure ngproteolytic activity (Kalisz, “Microbial Proteinases,” In: Fiechter(ed.), Advances in Biochemical Engineering/Biotechnology, (1988)). Forexample, proteolytic activity may be ascertained by comparative assayswhich analyze the respective protease's ability to hydrolyze acommercial substrate. Exemplary substrates useful in the analysis ofprotease or proteolytic activity, include, but are not limited to,di-methyl casein (Sigma C-9801), bovine collagen (Sigma C-9879), bovineelastin (Sigma E-1625), and Keratin Azure (Sigma-Aldrich K8500).Colorimetric assays utilizing these substrates are well known in the art(see, e.g., WO 99/34011 and U.S. Pat. No. 6,376,450, both of which areincorporated herein by reference).

Serine proteases are enzymes (EC No. 3.4.21) possessing an active siteserine that initiates hydrolysis of peptide bonds of proteins. Serineproteases comprise a diverse class of enzymes having a wide range ofspecificities and biological functions that are further divided based ontheir structure into chymotrypsin-like (trypsin-like) andsubtilisin-like. The prototypical subtilisin (EC No. 3.4.21.62) wasinitially obtained from Bacillus subtilis. Subtilisins (also sometimesreferred to as subtilases) and their homologues are members of the S8peptidase family of the MEROPS classification scheme. Members of familyS8 have a catalytic triad in the order Asp, His and Ser in their aminoacid sequence. Although a number of useful variant proteases have beendeveloped for cleaning applications, there remains a need for improvedsubtilisin variants.

BRIEF SUMMARY

In one embodiment, the present disclosure provides one or moresubtilisin variant having at least 70% amino acid sequence identity toSEQ ID NO: 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 22, wherethe variant has at least one, two, three, four, or more featuresselected from the group consisting of: X003T, X003V, X009E, X024Q,X040E, X069S, X076D, X078N, X079I, X087D, X118R, X124I, X128R, X128S,X129P, X130S, X145R, X166Q, X182E, X185Q, X210I, X211P, X217L, X218S,X248D, and X259P, where the positions are numbered by correspondencewith the amino acid sequence of SEQ ID NO:1 (BPN′), where the variantdoes not have 100% sequence identity to a naturally-occurring amino acidsequence.

In another embodiment, the disclosure provides one or more subtilisinvariant having at least 70% amino acid sequence identity to SEQ ID NO:8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 22, where the varianthas at least one, two or more features selected from the groupconsisting of X003V, X009E, X024Q, X040E, X069S, X076D, X078N, X079I,X087D, X118R, X124I, X128S, X129P, X130S, X145R, X166Q, X182E, X185Q,X210I, X217L, X218S, X248D, and X259P, where the positions are numberedby correspondence with the amino acid sequence of SEQ ID NO:1 (BPN′),where the variant does not have 100% sequence identity to anaturally-occurring amino acid sequence.

In another embodiment, the disclosure provides one or more subtilisinvariant having at least 70% amino acid sequence identity to SEQ ID NO:8, 10, 13, 14, 16, 17, or 19, where the variant has at least one, two ormore features selected from the group consisting of X003V, X009E, X040E,X069S, X076D, X078N, X166Q, X185Q, X218S, and X259P, where the positionsare numbered by correspondence with the amino acid sequence of SEQ IDNO:1 (BPN′), where the variant does not have 100% sequence identity to anaturally-occurring amino acid sequence. In another embodiment, thedisclosure provides one or more subtilisin variant having at least 70%amino acid sequence identity to SEQ ID NO: 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, or 22, where the variant has at least one featureselected from the group consisting of X003V-X009E, X003V-X024Q,X003V-X040E, X003V-X069S, X003V-X076D, X003V-X078N, X003V-X079I,X003V-X087D, X003V-X118R, X003V-X124I, X003V-X128S, X003V-X129P,X003V-X130S, X003V-X145R, X003V-X166Q, X003V-X185Q, X003V-X210I,X003V-X217L, X003V-X218S, X003V-X248D, X003V-X259P, X009E-X024Q,X009E-X040E, X009E-X069S, X009E-X076D, X009E-X078N, X009E-X079I,X009E-X087D, X009E-X118R, X009E-X124I, X009E-X128S, X009E-X129P,X009E-X130S, X009E-X145R, X009E-X166Q, X009E-X185Q, X009E-X210I,X009E-X217L, X009E-X218S, X009E-X248D, X009E-X259P, X024Q-X040E,X024Q-X069S, X024Q-X076D, X024Q-X078N, X024Q-X079I, X024Q-X087D,X024Q-X118R, X024Q-X124I, X024Q-X128S, X024Q-X129P, X024Q-X130S,X024Q-X145R, X024Q-X166Q, X024Q-X185Q, X024Q-X210I, X024Q-X217L,X024Q-X218S, X024Q-X248D, X024Q-X259P, X040E-X069S, X040E-X076D,X040E-X078N, X040E-X079I, X040E-X087D, X040E-X118R, X040E-X124I,X040E-X128S, X040E-X129P, X040E-X130S, X040E-X145R, X040E-X166Q,X040E-X185Q, X040E-X210I, X040E-X217L, X040E-X218S, X040E-X248D,X040E-X259P, X069S-X076D, X069S-X078N, X069S-X079I, X069S-X087D,X069S-X118R, X069S-X124I, X069S-X128S, X069S-X129P, X069S-X130S,X069S-X145R, X069S-X166Q, X069S-X185Q, X069S-X210I, X069S-X217L,X069S-X218S, X069S-X248D, X069S-X259P, X076D-X078N, X076D-X079I,X076D-X087D, X076D-X118R, X076D-X124I, X076D-X128S, X076D-X129P,X076D-X130S, X076D-X145R, X076D-X166Q, X076D-X185Q, X076D-X210I,X076D-X217L, X076D-X218S, X076D-X248D, X076D-X259P, X078N-X079I,X078N-X087D, X078N-X118R, X078N-X124I, X078N-X128S, X078N-X129P,X078N-X130S, X078N-X145R, X078N-X166Q, X078N-X185Q, X078N-X210I,X078N-X217L, X078N-X218S, X078N-X248D, X078N-X259P, X079I-X087D,X079I-X118R, X079I-X124I, X079I-X128S, X079I-X129P, X079I-X130S,X079I-X145R, X079I-X166Q, X079I-X185Q, X079I-X210I, X079I-X217L,X079I-X218S, X079I-X248D, X079I-X259P, X087D-X118R, X087D-X124I,X087D-X128S, X087D-X129P, X087D-X130S, X087D-X145R, X087D-X166Q,X087D-X185Q, X087D-X210I, X087D-X217L, X087D-X218S, X087D-X248D,X087D-X259P, X118R-X124I, X118R-X128S, X118R-X129P, X118R-X130S,X118R-X145R, X118R-X166Q, X118R-X185Q, X118R-X210I, X118R-X217L,X118R-X218S, X118R-X248D, X118R-X259P, X124I-X128S, X124I-X129P,X124I-X130S, X124I-X145R, X124I-X166Q, X124I-X185Q, X124I-X210I,X124I-X217L, X124I-X218S, X124I-X248D, X124I-X259P, X128S-X129P,X128S-X130S, X128S-X145R, X128S-X166Q, X128S-X185Q, X128S-X210I,X128S-X217L, X128S-X218S, X128S-X248D, X128S-X259P, X129P-X130S,X129P-X145R, X129P-X166Q, X129P-X185Q, X129P-X210I, X129P-X217L,X129P-X218S, X129P-X248D, X129P-X259P, X130S-X145R, X130S-X166Q,X130S-X185Q, X130S-X210I, X130S-X217L, X130S-X218S, X130S-X248D,X130S-X259P, X145R-X166Q, X145R-X185Q, X145R-X210I, X145R-X217L,X145R-X218S, X145R-X248D, X145R-X259P, X166Q-X185Q, X166Q-X210I,X166Q-X217L, X166Q-X218S, X166Q-X248D, X166Q-X259P, X185Q-X210I,X185Q-X217L, X185Q-X218S, X185Q-X248D, X185Q-X259P, X210I-X217L,X210I-X218S, X210I-X248D, X210I-X259P, X217L-X218S, X217L-X248D,X217L-X259P, X218S-X248D, X218S-X259P, and X248D-X259P, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′), where the variant does not have 100% sequenceidentity to a naturally-occurring amino acid sequence.

Some further embodiments are directed to a composition comprising one ormore subtilisin variant described herein. Further embodiments aredirected to a method of cleaning comprising contacting a surface or anitem in need of cleaning with an effective amount of one or moresubtilisin variant described herein or one or more composition describedherein.

Still other embodiments are directed to a method for producing a variantdescribed herein, comprising stably transforming a host cell with anexpression vector comprising a polynucleotide encoding one or moresubtilisin variant described herein. Still further embodiments aredirected to a polynucleotide comprising a nucleic acid sequence encodingone or more subtilisin variant described herein.

DESCRIPTION OF THE DRAWINGS

FIG. 1 depicts the locations on the structure of AprE (Subtilisin E fromB. subtilis, strain 168) (PDB entry 1SCJ) for a subset of sites wherecertain amino acid residues evaluated in this study show benefit inincreasing stability. The main chain fold of AprE (Subtilisin E) isschematically represented in light gray (only mature polypeptide regionis shown, excluding the propeptide segment), the catalytic tried isshown as gray spheres, and the sites evaluated for stability improvementare shown as black stick figures (numbered with respect to BPN′subtilisin sequence, SEQ ID NO:1).

FIG. 2 depicts the locations on a structural homology model of Bacillussp LG12 SprC subtilisin (described in WO2015038792) for a subset ofsites where certain amino acid residues evaluated in this study showbenefit in increasing stability. The main chain fold of LG12 isschematically represented in light gray, the catalytic triad is shown asgray spheres, and the sites evaluated for stability improvement areshown as black stick figures (numbered with respect to BPN′ subtilisinsequence). The subtilisins Chemgen_164A, CP474, and ZP-00454 evaluatedin this study are close homologs of LG12 (with amino acid sequenceidentity of 81.8%, 79.6% and 90.2%, respectively) and would be expectedto adopt a similar fold.

FIG. 3 depicts the locations on a structural homology model of B.gibsonii DSM14391 subtilisin for a subset of sites where certain aminoacid residues evaluated in this study show benefit in increasingstability. The homology model was built based on the structure ofBSP-00801 (described in WO2016205755), which is a variant of theBgi02446 subtilisin from B. gibsonii clade. The DSM14391 subtilisin,evaluated in this study is a close homolog of the Bgi02446 subtilisinand of the BSP-00801 variant subtilisin (with amino acid sequenceidentity of 90% and 89.6%, respectively). The main chain fold ofDSM14391 is schematically represented in light gray, the catalytic triadis shown as gray spheres, and the sites evaluated for stabilityimprovement are shown as black stick figures (numbered with respect toBPN′ subtilisin sequence).

FIG. 4 depicts the locations on the structure of BPN′ subtilisin from B.amyloliquefaciens (PDB entry 2ST1) for a subset of sites where certainamino acid residues evaluated in this study show benefit in increasingstability at corresponding positions in other subtilisins. The mainchain fold of BPN′ is schematically represented in light gray, thecatalytic triad is shown as gray spheres, and the sites evaluated forstability improvement are shown as black stick figures (numbered withrespect to BPN′ subtilisin sequence).

FIG. 5 depicts the locations on the structure of AprL (subtilisinCarlsberg) from B. licheniformis (PDB entry 1CSE) for a subset of siteswhere certain amino acid residues evaluated in this study show benefitin increasing stability at corresponding positions in other subtilisins.The main chain fold of AprL is schematically represented in light gray,the catalytic triad is shown as gray spheres, and the sites evaluatedfor stability improvement are shown as black stick figures (numberedwith respect to BPN′ subtilisin sequence).

FIG. 6 depicts the locations on the structure of B. lentus GG36subtilisin (PDB entry 1JEA) for a subset of sites where certain aminoacid residues evaluated in this study show benefit in increasingstability at corresponding positions in other subtilisins, includingBpan01744 (with amino acid sequence identity of 89.6%). The main chainfold of GG36 is schematically represented in light gray, the catalytictriad is shown as gray spheres, and the sites evaluated for stabilityimprovement are shown as black stick figures (numbered with respect toBPN′ subtilisin sequence).

DETAILED DESCRIPTION

The present disclosure provides subtilisin variants having amino acidsequences with one, two, three or more features (e.g. substitutions) atpositions in the polypeptide sequence that provide for improvedstability of the variant subtilisin when compared to a referencesubtilisin lacking the one, two, three, or more features. As provided inmore detail below, the features are found at positions selected from 3,9, 24, 40, 69, 76, 78, 79, 87, 118, 124, 128, 129, 130, 145, 166, 182,185, 210, 211, 217, 218, 248, and 259, where positions are numbered bycorrespondence to the amino acid positions of BPN′ (SEQ ID NO: 1) usingthe multiple protein sequence alignment shown on Table 28 of thisapplication. The features can be combinations at the positions listedabove, and include substitutions or, in some cases, combinations ofwildtype amino acids and substitutions at the identified positions thatprovide improved stability in comparison to a parent or referencesubtilisin polypeptide. Also provided are compositions (e.g. enzymecompositions or detergent compositions (e.g. dishwashing and laundrydetergent compositions)) containing such subtilisin variants and methodsusing such variants and compositions.

Terms and abbreviations not defined should be accorded their ordinarymeaning as used in the art. Unless defined otherwise herein, alltechnical and scientific terms used herein have the same meaning ascommonly understood by one of ordinary skill in the art. Any definitionsprovided herein are to be interpreted in the context of thespecification as a whole. As used herein, the singular “a,” “an” and“the” includes the plural unless the context clearly indicatesotherwise. Unless otherwise indicated, nucleic acid sequences arewritten left to right in 5′ to 3′ orientation; and amino acid sequencesare written left to right in amino to carboxy orientation. Eachnumerical range used herein includes every narrower numerical range thatfalls within such broader numerical range, as if such narrower numericalranges were all expressly written herein.

As used herein in connection with a numerical value, the term “about”refers to a range of +/−0.5 of the numerical value, unless the term isotherwise specifically defined in context. For instance, the phrase a“pH value of about 6” refers to pH values of from 5.5 to 6.5, unless thepH value is specifically defined otherwise.

The nomenclature of the amino acid substitutions of the one or moresubtilisin variants described herein uses one or more of the following:position; position:amino acid or amino acid substitution(s); or startingamino acid(s):position:amino acid substitution(s). Reference to a“position” (i.e. 5, 8, 17, 22, etc) encompasses any starting amino acidthat may be present at such position, and any substitution that may bepresent at such position. Reference to a position can be recited inseveral forms, for example, position 003 can also be referred to asposition 3. Reference to a “position: amino acid substitution(s)” (i.e.1S/T/G, 3G, 17T, etc) encompasses any starting amino acid that may bepresent at such position and the one or more amino acid(s) with whichsuch starting amino acid may be substituted. Reference to a starting orsubstituted amino acid may be further expressed as several starting, orsubstituted amino acids separated by a foreslash (“/”). For example,D275S/K indicates position 275 is substituted with serine (S) or lysine(K) and P/S197K indicates that starting amino acid proline (P) or serine(S) at position 197 is substituted with lysine (K). Reference to an X asthe amino acid in a position, refers to any amino acid at the recitedposition.

Unless otherwise indicated, the position of an amino acid residue in agiven amino acid sequence is numbered by correspondence with the aminoacid sequence of SEQ ID NO:1. That is, the amino acid sequence of BPN′shown in SEQ ID NO:1 serves as a reference sequence. In one embodiment,the amino acid sequence of one or more subtilisin variant describedherein is aligned with the amino acid sequence of SEQ ID NO:1 inaccordance with Table 28 using an alignment algorithm as describedherein, and each amino acid residue in the given amino acid sequencethat aligns (preferably optimally aligns) with an amino acid residue inSEQ ID NO:1 is conveniently numbered by reference to the numericalposition of that corresponding amino acid residue. Sequence alignmentalgorithms, such as, for example, those described herein will identifythe location or locations where insertions or deletions occur in asubject sequence when compared to a query sequence (also sometimesreferred to as “reference sequence”).

The terms “protease” and “proteinase” refer to an enzyme that has theability to break down proteins and peptides. A protease has the abilityto conduct “proteolysis,” by hydrolysis of peptide bonds that link aminoacids together in a peptide or polypeptide chain forming the protein.This activity of a protease as a protein-digesting enzyme is referred toas “proteolytic activity.” Many well-known procedures exist formeasuring proteolytic activity. For example, proteolytic activity may beascertained by comparative assays that analyze the respective protease'sability to hydrolyze a suitable substrate. Exemplary substrates usefulin the analysis of protease or proteolytic activity, include, but arenot limited to, di-methyl casein (Sigma C-9801), bovine collagen (SigmaC-9879), bovine elastin (Sigma E-1625), and Keratin Azure (Sigma-AldrichK8500). Colorimetric assays utilizing these substrates are well known inthe art (See e.g., WO99/34011 and U.S. Pat. No. 6,376,450). The pNApeptidyl assay (See e.g., Del Mar et al., Anal Biochem, 99:316-320,1979) also finds use in determining the active enzyme concentration.This assay measures the rate at which p-nitroaniline is released as theenzyme hydrolyzes a soluble synthetic substrate, such assuccinyl-alanine-alanine-proline-phenylalanine-p-nitroanilide(suc-AAPF-pNA). The rate of production of yellow color from thehydrolysis reaction is measured at 405 or 410 nm on a spectrophotometerand is proportional to the active enzyme concentration. In addition,absorbance measurements at 280 nanometers (nm) can be used to determinethe total protein concentration in a sample of purified protein. Theactivity on substrate divided by protein concentration gives the enzymespecific activity.

The phrase “composition(s) substantially-free of boron” or “detergent(s)substantially-free of boron” refers to composition(s) or detergent(s),respectively, that contain trace amounts of boron, for example, lessthan about 1000 ppm (1 mg/kg or liter equals 1 ppm), less than about 100ppm, less than about 50 ppm, less than about 10 ppm, or less than about5 ppm, or less than about 1 ppm, perhaps from other compositions ordetergent constituents.

As used herein, “the genus Bacillus” includes all species within thegenus “Bacillus,” as known to those of skill in the art, including butnot limited to B. subtilis, B. licheniformis, B. lentus, B. brevis, B.stearothermophilus, B. alkalophilus, B. amyloliquefaciens, B. clausii,B. halodurans, B. megaterium, B. coagulans, B. circulans, B. gibsonii,and B. thuringiensis. It is recognized that the genus Bacillus continuesto undergo taxonomical reorganization. Thus, it is intended that thegenus include species that have been reclassified, including but notlimited to such organisms as B. stearothermophilus, which is now named“Geobacillus stearothermophilus”, or B. polymyxa, which is now“Paenibacillus polymyxa”. The production of resistant endospores understressful environmental conditions is considered the defining feature ofthe genus Bacillus, although this characteristic also applies to therecently named Alicyclobacillus, Amphibacillus, Aneurinibacillus,Anoxybacillus, Brevibacillus, Filobacillus, Gracilibacillus,Halobacillus, Paenibacillus, Salibacillus, Thermobacillus, Ureibacillus,and Virgibacillus.

The term “vector” refers to a nucleic acid construct used to introduceor transfer nucleic acid(s) into a target cell or tissue. A vector istypically used to introduce foreign DNA into a cell or tissue. Vectorsinclude plasmids, cloning vectors, bacteriophages, viruses (e.g., viralvector), cosmids, expression vectors, shuttle vectors, and the like. Avector typically includes an origin of replication, a multicloning site,and a selectable marker. The process of inserting a vector into a targetcell is typically referred to as transformation. The present inventionincludes, in some embodiments, a vector that comprises a DNA sequenceencoding a serine protease polypeptide (e.g., precursor or mature serineprotease polypeptide) that is operably linked to a suitable prosequence(e.g., secretory, signal peptide sequence, etc.) capable of effectingthe expression of the DNA sequence in a suitable host, and the foldingand translocation of the recombinant polypeptide chain.

As used herein in the context of introducing a nucleic acid sequenceinto a cell, the term “introduced” refers to any method suitable fortransferring the nucleic acid sequence into the cell. Such methods forintroduction include but are not limited to protoplast fusion,transfection, transformation, electroporation, conjugation, andtransduction. Transformation refers to the genetic alteration of a cellwhich results from the uptake, optional genomic incorporation, andexpression of genetic material (e.g., DNA).

The term “expression” refers to the transcription and stableaccumulation of sense (mRNA) or anti-sense RNA, derived from a nucleicacid molecule of the disclosure. Expression may also refer totranslation of mRNA into a polypeptide. Thus, the term “expression”includes any step involved in the “production of the polypeptide”including, but not limited to, transcription, post-transcriptionalmodifications, translation, post-translational modifications, secretionand the like.

The phrases “expression cassette” or “expression vector” refer to anucleic acid construct or vector generated recombinantly orsynthetically for the expression of a nucleic acid of interest (e.g., aforeign nucleic acid or transgene) in a target cell. The nucleic acid ofinterest typically expresses a protein of interest. An expression vectoror expression cassette typically comprises a promoter nucleotidesequence that drives or promotes expression of the foreign nucleic acid.The expression vector or cassette also typically includes otherspecified nucleic acid elements that permit transcription of aparticular nucleic acid in a target cell. A recombinant expressioncassette can be incorporated into a plasmid, chromosome, mitochondrialDNA, plastid DNA, virus, or nucleic acid fragment. Some expressionvectors have the ability to incorporate and express heterologous DNAfragments in a host cell or genome of the host cell. Many prokaryoticand eukaryotic expression vectors are commercially available. Selectionof appropriate expression vectors for expression of a protein from anucleic acid sequence incorporated into the expression vector is withinthe knowledge of those of skill in the art.

As used herein, a nucleic acid is “operably linked” with another nucleicacid sequence when it is placed into a functional relationship withanother nucleic acid sequence. For example, a promoter or enhancer isoperably linked to a nucleotide coding sequence if the promoter affectsthe transcription of the coding sequence. A ribosome binding site may beoperably linked to a coding sequence if it is positioned so as tofacilitate translation of the coding sequence. Typically, “operablylinked” DNA sequences are contiguous. However, enhancers do not have tobe contiguous. Linking is accomplished by ligation at convenientrestriction sites. If such sites do not exist, synthetic oligonucleotideadaptors or linkers may be used in accordance with conventionalpractice.

The term “gene” refers to a polynucleotide (e.g., a DNA segment), thatencodes a polypeptide and includes regions preceding and following thecoding regions. In some instances a gene includes intervening sequences(introns) between individual coding segments (exons).

The term “recombinant”, when used with reference to a cell typicallyindicates that the cell has been modified by the introduction of aforeign nucleic acid sequence or that the cell is derived from a cell somodified. For example, a recombinant cell may comprise a gene not foundin identical form within the native (non-recombinant) form of the cell,or a recombinant cell may comprise a native gene (found in the nativeform of the cell) that has been modified and re-introduced into thecell. A recombinant cell may comprise a nucleic acid endogenous to thecell that has been modified without removing the nucleic acid from thecell; such modifications include those obtained by gene replacement,site-specific mutation, and related techniques known to those ofordinary skill in the art. Recombinant DNA technology includestechniques for the production of recombinant DNA in vitro and transferof the recombinant DNA into cells where it may be expressed orpropagated, thereby producing a recombinant polypeptide. “Recombination”and “recombining” of polynucleotides or nucleic acids refer generally tothe assembly or combining of two or more nucleic acid or polynucleotidestrands or fragments to generate a new polynucleotide or nucleic acid.

A nucleic acid or polynucleotide is said to “encode” a polypeptide if,in its native state or when manipulated by methods known to those ofskill in the art, it can be transcribed and/or translated to produce thepolypeptide or a fragment thereof. The anti-sense strand of such anucleic acid is also said to encode the sequence.

The terms “host strain” and “host cell” refer to a suitable host for anexpression vector comprising a DNA sequence of interest.

A “protein” or “polypeptide” comprises a polymeric sequence of aminoacid residues. The terms “protein” and “polypeptide” are usedinterchangeably herein. The single and three-letter code for amino acidsas defined in conformity with the IUPAC-IUB Joint Commission onBiochemical Nomenclature (JCBN) is used throughout this disclosure. Thesingle letter X refers to any of the twenty amino acids. It is alsounderstood that a polypeptide may be coded for by more than onenucleotide sequence due to the degeneracy of the genetic code.

The terms “prosequence” or “propeptide sequence” refer to an amino acidsequence between the signal peptide sequence and mature proteasesequence that is involved in the proper folding and secretion of theprotease; they are sometimes referred to as intramolecular chaperones.Cleavage of the prosequence or propeptide sequence results in a matureactive protease. Bacterial serine proteases are often expressed aspro-enzymes. Examples of modified propeptides are provided, for example,in WO 2016/205710.

The terms “signal sequence” and “signal peptide” refer to a sequence ofamino acid residues that may participate in the secretion or directtransport of the mature or precursor form of a protein. The signalsequence is typically located N-terminal to the precursor or matureprotein sequence. The signal sequence may be endogenous or exogenous. Asignal sequence is normally absent from the mature protein. A signalsequence is typically cleaved from the protein by a signal peptidaseafter the protein is transported.

The term “mature” form of a protein, polypeptide, or peptide refers tothe functional form of the protein, polypeptide, or peptide without thesignal peptide sequence and propeptide sequence.

The term “precursor” form of a protein or peptide refers to a matureform of the protein having a prosequence operably linked to the amino orcarbonyl terminus of the protein. The precursor may also have a “signal”sequence operably linked to the amino terminus of the prosequence. Theprecursor may also have additional polypeptides that are involved inpost-translational activity (e.g., polypeptides cleaved therefrom toleave the mature form of a protein or peptide).

The term “wildtype”, with respect to a polypeptide, refers to anaturally-occurring polypeptide that does not include a man-madesubstitution, insertion, or deletion at one or more amino acidpositions. Similarly, the term “wildtype”, with respect to apolynucleotide, refers to a naturally-occurring polynucleotide that doesnot include a man-made substitution, insertion, or deletion at one ormore nucleotides. A polynucleotide encoding a wildtype polypeptide is,however, not limited to a naturally-occurring polynucleotide, andencompasses any polynucleotide encoding the wildtype or parentalpolypeptide.

The term “parent”, with respect to a polypeptide, includes reference toa naturally-occurring, or wildtype, polypeptide or to anaturally-occurring polypeptide in which a man-made substitution,insertion, or deletion at one or more amino acid positions has beenmade. The term “parent” with respect to a polypeptide also includes anypolypeptide that has protease activity that serves as the startingpolypeptide for alteration, such as substitutions, additions, and/ordeletions, to result in a variant having one or more alterations incomparison to the starting polypeptide. That is, a parental, orreference polypeptide is not limited to a naturally-occurring wildtypepolypeptide, and encompasses any wildtype, parental, or referencepolypeptide. Similarly, the term “parent,” with respect to apolynucleotide, can refer to a naturally-occurring polynucleotide or toa polynucleotide that does include a man-made substitution, insertion,or deletion at one or more nucleotides. The term “parent” with respectto a polynucleotide also includes any polynucleotide that encodes apolypeptide having protease activity that serves as the startingpolynucleotide for alteration to result in a variant protease having amodification, such as substitutions, additions, and/or deletions, incomparison to the starting polynucleotide. That is, a polynucleotideencoding a wildtype, parental, or reference polypeptide is not limitedto a naturally-occurring polynucleotide, and encompasses anypolynucleotide encoding the wildtype, parental, or referencepolypeptide.

The term “naturally-occurring” refers to, for example, a sequence andresidues contained therein (e.g., polypeptide sequence and amino acidscontained therein or nucleic acid sequence and nucleotides containedtherein) that are found in nature. Conversely, the term “non-naturallyoccurring” refers to, for example, a sequence and residues containedtherein (e.g., polypeptide sequences and amino acids contained thereinor nucleic acid sequence and nucleotides contained therein) that are notfound in nature.

As used herein with regard to amino acid residue positions,“corresponding to” or “corresponds to” or “corresponds” refers to anamino acid residue at the enumerated position in a protein or peptide,or an amino acid residue that is analogous, homologous, or equivalent toan enumerated residue in a protein or peptide. As used herein,“corresponding region” generally refers to an analogous position in arelated protein or a reference protein.

The terms “derived from” and “obtained from” refer to not only a proteinproduced or producible by a strain of the organism in question, but alsoa protein encoded by a DNA sequence isolated from such strain andproduced in a host organism containing such DNA sequence. Additionally,the term refers to a protein which is encoded by a DNA sequence ofsynthetic and/or cDNA origin and which has the identifyingcharacteristics of the protein in question. To exemplify, “proteasesderived from Bacillus” refers to those enzymes having proteolyticactivity that are naturally produced by Bacillus, as well as to serineproteases like those produced by Bacillus sources but which through theuse of genetic engineering techniques are produced by other host cellstransformed with a nucleic acid encoding the serine proteases.

The term “identical” in the context of two polynucleotide or polypeptidesequences refers to nucleotides or amino acids in the two sequences thatare the same when aligned for maximum correspondence, as measured usingsequence comparison or analysis algorithms described below and known inthe art.

The phrases “% identity” or “percent identity” or “PID” refer to proteinsequence identity. Percent identity may be determined using standardtechniques known in the art. The percent amino acid identity shared bysequences of interest can be determined by aligning the sequences todirectly compare the sequence information, e.g., by using a program suchas BLAST, MUSCLE, or CLUSTAL. The BLAST algorithm is described, forexample, in Altschul et al., J Mol Biol, 215:403-410 (1990) and Karlinet al., Proc Natl Acad Sci USA, 90:5873-5787 (1993). A percent (%) aminoacid sequence identity value is determined by the number of matchingidentical residues divided by the total number of residues of the“reference” sequence including any gaps created by the program foroptimal/maximum alignment. BLAST algorithms refer to the “reference”sequence as the “query” sequence.

As used herein, “homologous proteins” or “homologous proteases” refersto proteins that have distinct similarity in primary, secondary, and/ortertiary structure. Protein homology can refer to the similarity inlinear amino acid sequence when proteins are aligned. Homology can bedetermined by amino acid sequence alignment, e.g., using a program suchas BLAST, MUSCLE, or CLUSTAL. Homologous search of protein sequences canbe done using BLASTP and PSI-BLAST from NCBI BLAST with threshold(E-value cut-off) at 0.001. (Altschul et al., “Gapped BLAST and PSIBLAST a new generation of protein database search programs”, NucleicAcids Res, Set 1; 25(17):3389-402(1997)). The BLAST program uses severalsearch parameters, most of which are set to the default values. The NCBIBLAST algorithm finds the most relevant sequences in terms of biologicalsimilarity but is not recommended for query sequences of less than 20residues (Altschul et al., Nucleic Acids Res, 25:3389-3402, 1997 andSchaffer et al., Nucleic Acids Res, 29:2994-3005, 2001). Exemplarydefault BLAST parameters for a nucleic acid sequence searches include:Neighboring words threshold=11; E-value cutoff=10; ScoringMatrix=NUC.3.1 (match=1, mismatch=−3); Gap Opening=5; and GapExtension=2. Exemplary default BLAST parameters for amino acid sequencesearches include: Word size=3; E-value cutoff=10; ScoringMatrix=BLOSUM62; Gap Opening=11; and Gap extension=1. Using thisinformation, protein sequences can be grouped and/or a phylogenetic treebuilt therefrom. Amino acid sequences can be entered in a program suchas the Vector NTI Advance suite and a Guide Tree can be created usingthe Neighbor Joining (NJ) method (Saitou and Nei, Mol Biol Evol,4:406-425, 1987). The tree construction can be calculated using Kimura'scorrection for sequence distance and ignoring positions with gaps. Aprogram such as AlignX can display the calculated distance values inparentheses following the molecule name displayed on the phylogenetictree.

In embodiments where three-dimensional structures of proteins have beendetermined or homology models created, structurally homologous aminoacid positions between two or more molecules can be determined. Formolecules with significant structural similarities, it might be expectedthat introducing substitutions that confer improvement in one moleculeat structurally homologous sites in another molecule could confersimilar improvements in performance and/or stability to these molecules.Structurally homologous amino acid positions can be identified byperforming a structural alignment, which attempts to determine homologybetween two or more protein structures based on their shape andthree-dimensional conformation. Structural alignment can produce asuperposition of the atomic coordinate sets and a minimal root meansquare deviation between the structures. Examples of methods forcreating structural alignments are the distance alignment matrix method(DALI) (Holm L, Sander C (1996) “Mapping the protein universe”, Science,273 (5275): 595-603), combinatorial extension (CE) (Shindyalov, I. N.;Bourne P. E. (1998) “Protein structure alignment by incrementalcombinatorial extension (CE) of the optimal path”, Protein Engineering,11 (9): 739-747), and Sequential Structure Alignment Program (S SAP)(Taylor W R, Flores T P, Orengo C A (1994) “Multiple protein structurealignment”, Protein Sci., 3 (10): 1858-70). By combining multiplesequence alignments with structural alignments, structurally homologousamino acid positions can be identified in molecules for which thethree-dimensional structure has not been determined. Examples of methodsfor creating multiple sequence alignment-based structural alignments are3DCoffee (Poirot O et al (2004) “3DCoffee@igs: a web server forcombining sequences and structures into a multiple sequence alignment”Nucleic Acids Res., 2004 Jul. 1; 32:W37-40), PROMALS3D (Pei J et al.(2008) “PROMALS3D: a tool for multiple protein sequence and structurealignments.” Nucleic Acids Res., 36(7):2295-300), and 3DM (Kuipers, R Ket al (2010) “3DM: Systematic analysis of heterogeneous superfamily datato discover protein functionalities” Proteins, 78(9):2101-13).Understanding the homology between molecules can reveal the evolutionaryhistory of the molecules, as well as information about their function;if a newly sequenced protein is homologous to an already characterizedprotein, there is a strong indication of the new protein's biochemicalfunction. Two molecules are said to be homologous if they have beenderived from a common ancestor. Homologous molecules, or homologs, canbe divided into two classes, paralogs and orthologs. Paralogs arehomologs that are present within one species. Paralogs often differ intheir detailed biochemical functions. Orthologs are homologs that arepresent within different species and have very similar or identicalfunctions. A protein superfamily is the largest grouping (clade) ofproteins for which common ancestry can be inferred. Usually this commonancestry is based on sequence alignment and mechanistic similarity.Superfamilies typically contain several protein families which showsequence similarity within the family. The term “protein clan” iscommonly used for protease superfamilies based on the MEROPS proteaseclassification system. As used herein, the term “subtilisin” includesany member of the S8 serine protease family as described in MEROPS—ThePeptidase Data base (Rawlings, N. D. et al (2016) Twenty years of theMEROPS database of proteolytic enzymes, their substrates and inhibitors.Nucleic Acids Res 44, D343-D350).

The CLUSTAL W algorithm is another example of a sequence alignmentalgorithm (See, Thompson et al., Nucleic Acids Res, 22:4673-4680, 1994).Default parameters for the CLUSTAL W algorithm include: Gap openingpenalty=10.0; Gap extension penalty=0.05; Protein weight matrix=BLOSUMseries; DNA weight matrix=IUB; Delay divergent sequences %=40; Gapseparation distance=8; DNA transitions weight=0.50; List hydrophilicresidues=GPSNDQEKR; Use negative matrix=OFF; Toggle Residue specificpenalties=ON; Toggle hydrophilic penalties=ON; and Toggle end gapseparation penalty=OFF. In CLUSTAL algorithms, deletions occurring ateither terminus are included. For example, a variant with a five aminoacid deletion at either terminus (or within the polypeptide) of apolypeptide of 500 amino acids would have a percent sequence identity of99% (495/500 identical residues x 100) relative to the “reference”polypeptide. Such a variant would be encompassed by a variant having “atleast 99% sequence identity” to the polypeptide.

A nucleic acid or polynucleotide is “isolated” when it is at leastpartially or completely separated from other components, including butnot limited to for example, other proteins, nucleic acids, cells, etc.Similarly, a polypeptide, protein or peptide is “isolated” when it is atleast partially or completely separated from other components, includingbut not limited to for example, other proteins, nucleic acids, cells,etc. On a molar basis, an isolated species is more abundant than areother species in a composition. For example, an isolated species maycomprise at least about 50%, about 55%, about 60%, about 65%, about 70%,about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%,or about 100% (on a molar basis) of all macromolecular species present.Preferably, the species of interest is purified to essential homogeneity(i.e., contaminant species cannot be detected in the composition byconventional detection methods). Purity and homogeneity can bedetermined using a number of techniques well known in the art, such asagarose or polyacrylamide gel electrophoresis of a nucleic acid or aprotein sample, respectively, followed by visualization upon staining.If desired, a high-resolution technique, such as high performance liquidchromatography (HPLC) or a similar means can be utilized forpurification of the material.

The term “purified” as applied to nucleic acids or polypeptidesgenerally denotes a nucleic acid or polypeptide that is essentially freefrom other components as determined by analytical techniques well knownin the art (e.g., a purified polypeptide or polynucleotide forms adiscrete band in an electrophoretic gel, chromatographic eluate, and/ora media subjected to density gradient centrifugation). For example, anucleic acid or polypeptide that gives rise to essentially one band inan electrophoretic gel is “purified.” A purified nucleic acid orpolypeptide is at least about 50% pure, usually at least about 60%,about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%,about 98%, about 99%, about 99.5%, about 99.6%, about 99.7%, about 99.8%or more pure (e.g., percent by weight on a molar basis). In a relatedsense, a composition is enriched for a molecule when there is asubstantial increase in the concentration of the molecule afterapplication of a purification or enrichment technique. The term“enriched” refers to a compound, polypeptide, cell, nucleic acid, aminoacid, or other specified material or component that is present in acomposition at a relative or absolute concentration that is higher thanin a starting composition.

The term “cleaning activity” refers to a cleaning performance achievedby a serine protease polypeptide, variant, or reference subtilisin underconditions prevailing during the proteolytic, hydrolyzing, cleaning, orother process of the disclosure. In some embodiments, cleaningperformance of a serine protease or reference subtilisin may bedetermined by using various assays for cleaning one or more enzymesensitive stain on an item or surface (e.g., a stain resulting fromfood, grass, blood, ink, milk, oil, and/or egg protein). Cleaningperformance of one or more subtilisin variant described herein orreference subtilisin can be determined by subjecting the stain on theitem or surface to standard wash condition(s) and assessing the degreeto which the stain is removed by using various chromatographic,spectrophotometric, or other quantitative methodologies. Exemplarycleaning assays and methods are known in the art and include, but arenot limited to those described in WO99/34011 and U.S. Pat. No.6,605,458, as well as those cleaning assays and methods included in theExamples provided below.

The terms “stable” and “stability” with regard to a protease variantrefer to a protease that retains a greater amount of residual activitywhen compared to the parent or reference protease after exposure toaltered temperatures over a given period of time under conditions (or“stress conditions”) prevailing during proteolytic, hydrolysing,cleaning or other process. Residual activity is the amount of activityremaining after the test compared to the initial activity of the sampleand can be reported as a percentage e.g. % remaining activity. “Alteredtemperatures” encompass increased or decreased temperatures. In someembodiments, the proteases retain at least about 10%, about 15%, about20%, about 25%, about 30%, about 35%, about 40%, about 50%, about 60%,about 70%, about 80%, about 85%, about 90%, about 92%, about 95%, about96%, about 97%, about 98%, or about 99% proteolytic activity (residualactivity) in comparison to the respective parent or reference proteaseafter exposure to altered temperatures over a given time period, forexample, at least about 20 minutes, at least about 40 minutes, at leastabout 60 minutes, about 90 minutes, about 120 minutes, about 180minutes, about 240 minutes, about 300 minutes, about 360 minutes, about420 minutes, about 480 minutes, about 540 minutes, about 600 minutes,about 660 minutes, about 720 minutes, about 780 minutes, about 840minutes, about 900 minutes, about 960 minutes, about 1020 minutes, about1080 minutes, about 1140 minutes, or about 1200 minutes.

Alternatively, the terms “stable” and “stability” with regard to aprotease variant also refer to a protease that, after exposure toaltered temperatures over a given period of time under conditions (or“stress conditions”) prevailing during proteolytic, hydrolysing,cleaning or other process, retains a higher residual activity than aparent, or reference, protease. “Altered temperatures” encompassincreased or decreased temperatures. A stability Performance Index (PI)for a variant protease can be obtained by dividing the residual activityof the variant protease by the residual activity of the parent, orreference protease when tested under the same conditions, stressed andnon-stressed. In some embodiments, the protease variants have a PI ofabout 1.1, about 1.2, about 1.3, about 1.4, about 1.5, about 2, about2.5, about 3, about 4, or higher than 4, after exposure to alteredtemperatures over a given time period, for example, at least about 5minutes, at least about 10 minutes, at least about 20 minutes, at leastabout 40 minutes, at least about 60 minutes, about 90 minutes, about 120minutes, about 180 minutes, about 240 minutes, about 300 minutes, about360 minutes, about 420 minutes, about 480 minutes, about 540 minutes,about 600 minutes, about 660 minutes, about 720 minutes, about 780minutes, about 840 minutes, about 900 minutes, about 960 minutes, about1020 minutes, about 1080 minutes, about 1140 minutes, or about 1200minutes. Altered temperatures for evaluation of protein stability can bebetween 28-85° C., e.g. 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, or 80°C. In some embodiments, stability (e.g. residual activity or performanceindex) may be measured in the presence of one or more proteasestabilizers.

Alternatively, the terms “stable” and “stability” with regard to aprotease variant also refer to a protease that, after exposure toaltered temperatures over a given period of time under conditions (or“stress conditions”) prevailing during proteolytic, hydrolysing,cleaning or other process, exhibits longer half-lives for inactivation(T1/2) than a parent, or reference, protease. “Altered temperatures”encompass increased or decreased temperatures. “Half-lives forinactivation” with regard to a protease variant refers to the timeperiod after which the protease retains one half of the initialenzymatic activity.

The term “stability” includes storage stability and stability duringuse, e.g. during a wash process and reflects the stability of thesubtilisin variant according to the invention as a function of time,e.g. how much activity is retained when the subtilisin variants is keptin solution in particular in a detergent solution. The stability isinfluenced by many factors e.g. pH, temperature, detergent composition,e.g. amount of builder, surfactant, water content, proteaseinhibitors/stabilizers etc. The stability of the subtilisin variant maybe measured using the assays described in Example 2. The term “improvedstability” or “increased stability” is defined herein as a variantsubtilisin displaying an increased stability in solutions, relative tothe stability of the parent subtilisin. The terms “improved stability”and “increased stability” includes “improved chemical stability” or“improved detergent stability”.

The term “improved detergent stability” is defined herein as a variantsubtilisin displaying retention of enzymatic activity after a period ofincubation in the presence of a detergent or chemical component of adetergent, which reduces the enzymatic activity of the parent enzyme.Improved detergent stability may also result in variants being more ableto catalyze a reaction in the presence of such detergent or chemicalcomponents. The term “detergent stability” or “improved detergentstability” is in particular an improved stability of the proteaseactivity when a subtilisin variant of the present invention is mixedinto a liquid detergent formulation and incubated at temperaturesbetween 30-70° C., e.g. 35, 40, 45, 50, 55, 60, or 65° C. Detergentstability can be evaluated in a diluted liquid detergent composition,such as 10% detergent, where the commercial liquid detergent is diluted10 fold in water or a liquid buffer solution prepared at a relevant pH.

The term “enhanced stability” or “improved stability” in the context ofan oxidation, chelator, denaturant, surfactant, thermal and/or pH stableprotease refers to a higher retained proteolytic activity over time ascompared to a reference protease, for example, a wildtype protease orparent protease. Autolysis has been identified as one mode of subtilisinactivity loss in liquid detergents. (Stoner et al., 2004 Proteaseautolysis in heavy-duty liquid detergent formulations: effects ofthermodynamic stabilizers and protease inhibitors, Enzyme and MicrobialTechnology 34:114-125.)

The term “effective amount” of one or more subtilisin variant describedherein or reference subtilisin refers to the amount of protease thatachieves a desired level of enzymatic activity in a specific cleaningcomposition. Such effective amounts are readily ascertained by one ofordinary skill in the art and are based on many factors, such as theparticular protease used, the cleaning application, the specificcomposition of the cleaning composition, and whether a liquid or dry(e.g., granular, tablet, bar) composition is required, etc.

The term “adjunct material” refers to any liquid, solid, or gaseousmaterial included in a cleaning composition, other than one or moresubtilisin variant described herein, or recombinant polypeptide oractive fragment thereof. In some embodiments, the cleaning compositionsof the present disclosure include one or more cleaning adjunctmaterials. Each cleaning adjunct material is typically selecteddepending on the particular type and form of cleaning composition (e.g.,liquid, granule, powder, bar, paste, spray, tablet, gel, foam, or othercomposition). Preferably, each cleaning adjunct material is compatiblewith the protease enzyme used in the composition.

Cleaning compositions and cleaning formulations include any compositionthat is suited for cleaning, bleaching, disinfecting, and/or sterilizingany object, item, and/or surface. Such compositions and formulationsinclude, but are not limited to, for example, liquid and/or solidcompositions, including cleaning or detergent compositions (e.g.,liquid, tablet, gel, bar, granule, and/or solid laundry cleaning ordetergent compositions and fine fabric detergent compositions); hardsurface cleaning compositions and formulations, such as for glass, wood,ceramic and metal counter tops and windows; carpet cleaners; ovencleaners; fabric fresheners; fabric softeners; and textile, laundrybooster cleaning or detergent compositions, laundry additive cleaningcompositions, and laundry pre-spotter cleaning compositions; dishwashingcompositions, including hand or manual dishwashing compositions (e.g.,“hand” or “manual” dishwashing detergents) and automatic dishwashingcompositions (e.g., “automatic dishwashing detergents”). Single dosageunit forms also find use with the present invention, including but notlimited to pills, tablets, gelcaps, or other single dosage units such aspre-measured powders or liquids.

Cleaning composition or cleaning formulations, as used herein, include,unless otherwise indicated, granular or powder-form all-purpose orheavy-duty washing agents, especially cleaning detergents; liquid,granular, gel, solid, tablet, paste, or unit dosage form all-purposewashing agents, especially the so-called heavy-duty liquid (HDL)detergent or heavy-duty dry (HDD) detergent types; liquid fine-fabricdetergents; hand or manual dishwashing agents, including those of thehigh-foaming type; hand or manual dishwashing, automatic dishwashing(ADW), or dishware or tableware washing agents, including the varioustablet, powder, solid, granular, liquid, gel, and rinse-aid types forhousehold and institutional use; liquid cleaning and disinfectingagents, including antibacterial hand-wash types, cleaning bars,mouthwashes, denture cleaners, car shampoos, carpet shampoos, bathroomcleaners; hair shampoos and/or hair-rinses for humans and other animals;shower gels and foam baths and metal cleaners; as well as cleaningauxiliaries, such as bleach additives and “stain-stick” or pre-treattypes. In some embodiments, granular compositions are in “compact” form;in some embodiments, liquid compositions are in a “concentrated” form.

The term “detergent composition” or “detergent formulation” is used inreference to a composition intended for use in a wash medium for thecleaning of soiled or dirty objects, including particular fabric and/ornon-fabric objects or items. In some embodiments, the detergents of thedisclosure comprise one or more subtilisin variant described herein and,in addition, one or more surfactants, transferase(s), hydrolyticenzymes, oxido reductases, builders (e.g., a builder salt), bleachingagents, bleach activators, bluing agents, fluorescent dyes, cakinginhibitors, masking agents, enzyme stabilizers, calcium, enzymeactivators, antioxidants, and/or solubilizers. In some instances, abuilder salt is a mixture of a silicate salt and a phosphate salt,preferably with more silicate (e.g., sodium metasilicate) than phosphate(e.g., sodium tripolyphosphate). Some embodiments are directed tocleaning compositions or detergent compositions that do not contain anyphosphate (e.g., phosphate salt or phosphate builder).

The term “bleaching” refers to the treatment of a material (e.g.,fabric, laundry, pulp, etc.) or surface for a sufficient length of timeand/or under appropriate pH and/or temperature conditions to effect abrightening (i.e., whitening) and/or cleaning of the material. Examplesof chemicals suitable for bleaching include, but are not limited to, forexample, ClO₂, H₂O₂, peracids, NO₂, etc. Bleaching agents also includeenzymatic bleaching agents such as perhydrolase and arylesterases.Another embodiment is directed to a composition comprising one or moresubtilisin variant described herein, and one or more perhydrolase, suchas, for example, is described in WO2005/056782, WO2007/106293, WO2008/063400, WO2008/106214, and WO2008/106215.

The term “wash performance” of a protease (e.g., one or more subtilisinvariant described herein, or recombinant polypeptide or active fragmentthereof) refers to the contribution of one or more subtilisin variantdescribed herein to washing that provides additional cleaningperformance to the detergent as compared to the detergent without theaddition of the one or more subtilisin variant described herein to thecomposition. Wash performance is compared under relevant washingconditions. In some test systems, other relevant factors, such asdetergent composition, sud concentration, water hardness, washingmechanics, time, pH, and/or temperature, can be controlled in such a waythat condition(s) typical for household application in a certain marketsegment (e.g., hand or manual dishwashing, automatic dishwashing,dishware cleaning, tableware cleaning, fabric cleaning, etc.) areimitated.

The phrase “relevant washing conditions” is used herein to indicate theconditions, particularly washing temperature, time, washing mechanics,sud concentration, type of detergent and water hardness, actually usedin households in a hand dishwashing, automatic dishwashing, or laundrydetergent market segment.

The term “disinfecting” refers to the removal of contaminants from thesurfaces, as well as the inhibition or killing of microbes on thesurfaces of items.

The term “compact” form of the cleaning compositions herein is bestreflected by density and, in terms of composition, by the amount ofinorganic filler salt. Inorganic filler salts are conventionalingredients of detergent compositions in powder form. In conventionaldetergent compositions, the filler salts are present in substantialamounts, typically about 17 to about 35% by weight of the totalcomposition. In contrast, in compact compositions, the filler salt ispresent in amounts not exceeding about 15% of the total composition. Insome embodiments, the filler salt is present in amounts that do notexceed about 10%, or more preferably, about 5%, by weight of thecomposition. In some embodiments, the inorganic filler salts areselected from the alkali and alkaline-earth-metal salts of sulfates andchlorides. In some embodiments, the filler salt is sodium sulfate.

Disclosed herein is one or more subtilisin variants useful, for example,in cleaning compositions and applications and in methods of cleaning, aswell as in a variety of industrial applications. Disclosed herein is oneor more isolated, recombinant, substantially pure, or non-naturallyoccurring subtilisin variants. In some embodiments, one or moresubtilisin variants described herein is useful in cleaning applicationsand can be incorporated into cleaning compositions that are useful inmethods of cleaning an item or a surface in need thereof.

In one embodiment, the disclosure provides one or more subtilisinvariant having at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%,95%, 96%, 97%, 98%, or 99% amino acid sequence identity to SEQ ID NO: 8,9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 22, where the variant hasat least one, two, three, four, or more features selected from the groupconsisting of: X003T, X003V, X009E, X024Q, X040E, X069S, X076D, X078N,X079I, X087D, X118R, X124I, X128R, X128S, X129P, X130S, X145R, X166Q,X182E, X185Q, X210I, X211P, X217L, X218S, X248D, and X259P, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′). In one embodiment, the variant does not have 100%sequence identity to a wildtype amino acid sequence (SEQ ID NO: 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 22).

In another embodiment, the disclosure provides one or more subtilisinvariants having at least one, two, three or more features selected fromthe group consisting of X003V, X009E, X024Q, X040E, X069S, X076D, X078N,X079I, X087D, X118R, X124I, X128S, X129P, X130S, X166Q, X182E, X185Q,X217L, X218S, X248D, and X259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In another embodiment, the subtilisin variant has at least one, two,three or more features selected from the group consisting of X003V,X009E, X040E, X069S, X076D, X078N, X166Q, X185Q, X218S, and X259P, wherethe positions are numbered by correspondence with the amino acidsequence of SEQ ID NO:1 (BPN′), where the variant does not have 100%sequence identity to a wildtype amino acid sequence.

In still another embodiment, the subtilisin variant has at least two ormore features, where the combination of two more features are selectedfrom the group consisting of X003V-X009E, X003V-X024Q, X003V-X040E,X003V-X069S, X003V-X076D, X003V-X078N, X003V-X079I, X003V-X087D,X003V-X118R, X003V-X124I, X003V-X128S, X003V-X129P, X003V-X130S,X003V-X145R, X003V-X166Q, X003V-X185Q, X003V-X210I, X003V-X217L,X003V-X218S, X003V-X248D, X003V-X259P, X009E-X024Q, X009E-X040E,X009E-X069S, X009E-X076D, X009E-X078N, X009E-X079I, X009E-X087D,X009E-X118R, X009E-X124I, X009E-X128S, X009E-X129P, X009E-X130S,X009E-X145R, X009E-X166Q, X009E-X185Q, X009E-X210I, X009E-X217L,X009E-X218S, X009E-X248D, X009E-X259P, X024Q-X040E, X024Q-X069S,X024Q-X076D, X024Q-X078N, X024Q-X079I, X024Q-X087D, X024Q-X118R,X024Q-X124I, X024Q-X128S, X024Q-X129P, X024Q-X130S, X024Q-X145R,X024Q-X166Q, X024Q-X185Q, X024Q-X210I, X024Q-X217L, X024Q-X218S,X024Q-X248D, X024Q-X259P, X040E-X069S, X040E-X076D, X040E-X078N,X040E-X079I, X040E-X087D, X040E-X118R, X040E-X124I, X040E-X128S,X040E-X129P, X040E-X130S, X040E-X145R, X040E-X166Q, X040E-X185Q,X040E-X210I, X040E-X217L, X040E-X218S, X040E-X248D, X040E-X259P,X069S-X076D, X069S-X078N, X069S-X079I, X069S-X087D, X069S-X118R,X069S-X124I, X069S-X128S, X069S-X129P, X069S-X130S, X069S-X145R,X069S-X166Q, X069S-X185Q, X069S-X210I, X069S-X217L, X069S-X218S,X069S-X248D, X069S-X259P, X076D-X078N, X076D-X079I, X076D-X087D,X076D-X118R, X076D-X124I, X076D-X128S, X076D-X129P, X076D-X130S,X076D-X145R, X076D-X166Q, X076D-X185Q, X076D-X210I, X076D-X217L,X076D-X218S, X076D-X248D, X076D-X259P, X078N-X079I, X078N-X087D,X078N-X118R, X078N-X124I, X078N-X128S, X078N-X129P, X078N-X130S,X078N-X145R, X078N-X166Q, X078N-X185Q, X078N-X210I, X078N-X217L,X078N-X218S, X078N-X248D, X078N-X259P, X079I-X087D, X079I-X118R,X079I-X124I, X079I-X128S, X079I-X129P, X079I-X130S, X079I-X145R,X079I-X166Q, X079I-X185Q, X079I-X210I, X079I-X217L, X079I-X218S,X079I-X248D, X079I-X259P, X087D-X118R, X087D-X124I, X087D-X128S,X087D-X129P, X087D-X130S, X087D-X145R, X087D-X166Q, X087D-X185Q,X087D-X210I, X087D-X217L, X087D-X218S, X087D-X248D, X087D-X259P,X118R-X124I, X118R-X128S, X118R-X129P, X118R-X130S, X118R-X145R,X118R-X166Q, X118R-X185Q, X118R-X210I, X118R-X217L, X118R-X218S,X118R-X248D, X118R-X259P, X124I-X128S, X124I-X129P, X124I-X130S,X124I-X145R, X124I-X166Q, X124I-X185Q, X124I-X210I, X124I-X217L,X124I-X218S, X124I-X248D, X124I-X259P, X128S-X129P, X128S-X130S,X128S-X145R, X128S-X166Q, X128S-X185Q, X128S-X210I, X128S-X217L,X128S-X218S, X128S-X248D, X128S-X259P, X129P-X130S, X129P-X145R,X129P-X166Q, X129P-X185Q, X129P-X210I, X129P-X217L, X129P-X218S,X129P-X248D, X129P-X259P, X130S-X145R, X130S-X166Q, X130S-X185Q,X130S-X210I, X130S-X217L, X130S-X218S, X130S-X248D, X130S-X259P,X145R-X166Q, X145R-X185Q, X145R-X210I, X145R-X217L, X145R-X218S,X145R-X248D, X145R-X259P, X166Q-X185Q, X166Q-X210I, X166Q-X217L,X166Q-X218S, X166Q-X248D, X166Q-X259P, X185Q-X210I, X185Q-X217L,X185Q-X218S, X185Q-X248D, X185Q-X259P, X210I-X217L, X210I-X218S,X210I-X248D, X210I-X259P, X217L-X218S, X217L-X248D, X217L-X259P,X218S-X248D, X218S-X259P, X248D-X259P where the positions are numberedby correspondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In other embodiments, the subtilisin variants disclosed herein contain acombination of two or more features with respect to SEQ ID NO: 1, wherethe combination of two or more features are selected from the groupconsisting of X003V-X009E, X003V-X040E, X003V-X069S, X003V-X076D,X003V-X078N, X003V-X079I, X003V-X124I, X003V-X128S, X003V-X129P,X003V-X166Q, X003V-X185Q, X003V-X218S, X003V-X259P, X003V-X262L,X009E-X040E, X009E-X069S, X009E-X076D, X009E-X078N, X009E-X166Q,X009E-X185Q, X009E-X218S, X009E-X259P, X040E-X069S, X040E-X076D,X040E-X078N, X040E-X079I, X040E-X124I, X040E-X128S, X040E-X129P,X040E-X166Q, X040E-X185Q, X040E-X218S, X040E-X259P, X069S-X076D,X069S-X078N, X069S-X079I, X069S-X124I, X069S-X128S, X069S-X129P,X069S-X166Q, X069S-X185Q, X069S-X218S, X069S-X259P, X076D-X078N,X076D-X079I, X076D-X124I, X076D-X128S, X076D-X129P, X076D-X166Q,X076D-X185Q, X076D-X218S, X076D-X259P, X078N-X079I, X078N-X124I,X078N-X128S, X078N-X129P, X078N-X166Q, X078N-X185Q, X078N-X218S,X078N-X259P, X078T-X124I, X079I-X124I, X079I-X128S, X079I-X129P,X079I-X166Q, X079I-X185Q, X079I-X218S, X079I-X259P, X124I-X128S,X124I-X129P, X124I-X166Q, X124I-X185Q, X124I-X218S, X124I-X259K,X124I-X259P, X128S-X129P, X128S-X166Q, X128S-X185Q, X128S-X218S,X128S-X259P, X129P-X166Q, X129P-X185Q, X129P-X218S, X129P-X259P,X166Q-X185Q, X166Q-X218S, X166Q-X259P, X185Q-X218S, X185Q-X259P, andX218S-X259P, where the positions are numbered by correspondence with theamino acid sequence of SEQ ID NO:1 (BPN′).

In other embodiments, the subtilisin variants disclosed herein contain acombination of three or more features with respect to SEQ ID NO: 1,where the combination of three or more features are selected from thegroup consisting of X003V-X009E-X024Q, X003V-X009E-X040E,X003V-X009E-X069S, X003V-X009E-X076D, X003V-X009E-X078N,X003V-X009E-X079I, X003V-X009E-X087D, X003V-X009E-X118R,X003V-X009E-X124I, X003V-X009E-X128S, X003V-X009E-X129P,X003V-X009E-X130S, X003V-X009E-X145R, X003V-X009E-X166Q,X003V-X009E-X185Q, X003V-X009E-X210I, X003V-X009E-X217L,X003V-X009E-X218S, X003V-X009E-X248D, X003V-X009E-X259P,X003V-X024Q-X040E, X003V-X024Q-X069S, X003V-X024Q-X076D,X003V-X024Q-X078N, X003V-X024Q-X079I, X003V-X024Q-X087D,X003V-X024Q-X118R, X003V-X024Q-X124I, X003V-X024Q-X128S,X003V-X024Q-X129P, X003V-X024Q-X130S, X003V-X024Q-X145R,X003V-X024Q-X166Q, X003V-X024Q-X185Q, X003V-X024Q-X210I,X003V-X024Q-X217L, X003V-X024Q-X218S, X003V-X024Q-X248D,X003V-X024Q-X259P, X003V-X040E-X069S, X003V-X040E-X076D,X003V-X040E-X078N, X003V-X040E-X079I, X003V-X040E-X087D,X003V-X040E-X118R, X003V-X040E-X124I, X003V-X040E-X128S,X003V-X040E-X129P, X003V-X040E-X130S, X003V-X040E-X145R,X003V-X040E-X166Q, X003V-X040E-X185Q, X003V-X040E-X210I,X003V-X040E-X217L, X003V-X040E-X218S, X003V-X040E-X248D,X003V-X040E-X259P, X003V-X069S-X076D, X003V-X069S-X078N,X003V-X069S-X079I, X003V-X069S-X087D, X003V-X069S-X118R,X003V-X069S-X124I, X003V-X069S-X128S, X003V-X069S-X129P,X003V-X069S-X130S, X003V-X069S-X145R, X003V-X069S-X166Q,X003V-X069S-X185Q, X003V-X069S-X210I, X003V-X069S-X217L,X003V-X069S-X218S, X003V-X069S-X248D, X003V-X069S-X259P,X003V-X076D-X078N, X003V-X076D-X079I, X003V-X076D-X087D,X003V-X076D-X118R, X003V-X076D-X124I, X003V-X076D-X128S,X003V-X076D-X129P, X003V-X076D-X130S, X003V-X076D-X145R,X003V-X076D-X166Q, X003V-X076D-X185Q, X003V-X076D-X210I,X003V-X076D-X217L, X003V-X076D-X218S, X003V-X076D-X248D,X003V-X076D-X259P, X003V-X078N-X079I, X003V-X078N-X087D,X003V-X078N-X118R, X003V-X078N-X124I, X003V-X078N-X128S,X003V-X078N-X129P, X003V-X078N-X130S, X003V-X078N-X145R,X003V-X078N-X166Q, X003V-X078N-X185Q, X003V-X078N-X210I,X003V-X078N-X217L, X003V-X078N-X218S, X003V-X078N-X248D,X003V-X078N-X259P, X003V-X079I-X087D, X003V-X079I-X118R,X003V-X079I-X124I, X003V-X079I-X128S, X003V-X079I-X129P,X003V-X079I-X130S, X003V-X079I-X145R, X003V-X079I-X166Q,X003V-X079I-X185Q, X003V-X079I-X210I, X003V-X079I-X217L,X003V-X079I-X218S, X003V-X079I-X248D, X003V-X079I-X259P,X003V-X087D-X118R, X003V-X087D-X124I, X003V-X087D-X128S,X003V-X087D-X129P, X003V-X087D-X130S, X003V-X087D-X145R,X003V-X087D-X166Q, X003V-X087D-X185Q, X003V-X087D-X210I,X003V-X087D-X217L, X003V-X087D-X218S, X003V-X087D-X248D,X003V-X087D-X259P, X003V-X118R-X124I, X003V-X118R-X128S,X003V-X118R-X129P, X003V-X118R-X130S, X003V-X118R-X145R,X003V-X118R-X166Q, X003V-X118R-X185Q, X003V-X118R-X210I,X003V-X118R-X217L, X003V-X118R-X218S, X003V-X118R-X248D,X003V-X118R-X259P, X003V-X124I-X128S, X003V-X124I-X129P,X003V-X124I-X130S, X003V-X124I-X145R, X003V-X124I-X166Q,X003V-X124I-X185Q, X003V-X124I-X210I, X003V-X124I-X217L,X003V-X124I-X218S, X003V-X124I-X248D, X003V-X124I-X259P,X003V-X128S-X129P, X003V-X128S-X130S, X003V-X128S-X145R,X003V-X128S-X166Q, X003V-X128S-X185Q, X003V-X128S-X210I,X003V-X128S-X217L, X003V-X128S-X218S, X003V-X128S-X248D,X003V-X128S-X259P, X003V-X129P-X130S, X003V-X129P-X145R,X003V-X129P-X166Q, X003V-X129P-X185Q, X003V-X129P-X210I,X003V-X129P-X217L, X003V-X129P-X218S, X003V-X129P-X248D,X003V-X129P-X259P, X003V-X130S-X145R, X003V-X130S-X166Q,X003V-X130S-X185Q, X003V-X130S-X210I, X003V-X130S-X217L,X003V-X130S-X218S, X003V-X130S-X248D, X003V-X130S-X259P,X003V-X145R-X166Q, X003V-X145R-X185Q, X003V-X145R-X210I,X003V-X145R-X217L, X003V-X145R-X218S, X003V-X145R-X248D,X003V-X145R-X259P, X003V-X166Q-X185Q, X003V-X166Q-X210I,X003V-X166Q-X217L, X003V-X166Q-X218S, X003V-X166Q-X248D,X003V-X166Q-X259P, X003V-X185Q-X210I, X003V-X185Q-X217L,X003V-X185Q-X218S, X003V-X185Q-X248D, X003V-X185Q-X259P,X003V-X210I-X217L, X003V-X210I-X218S, X003V-X210I-X248D,X003V-X210I-X259P, X003V-X217L-X218S, X003V-X217L-X248D,X003V-X217L-X259P, X003V-X218S-X248D, X003V-X218S-X259P,X003V-X248D-X259P, X009E-X024Q-X040E, X009E-X024Q-X069S,X009E-X024Q-X076D, X009E-X024Q-X078N, X009E-X024Q-X079I,X009E-X024Q-X087D, X009E-X024Q-X118R, X009E-X024Q-X124I,X009E-X024Q-X128S, X009E-X024Q-X129P, X009E-X024Q-X130S,X009E-X024Q-X145R, X009E-X024Q-X166Q, X009E-X024Q-X185Q,X009E-X024Q-X210I, X009E-X024Q-X217L, X009E-X024Q-X218S,X009E-X024Q-X248D, X009E-X024Q-X259P, X009E-X040E-X069S,X009E-X040E-X076D, X009E-X040E-X078N, X009E-X040E-X079I,X009E-X040E-X087D, X009E-X040E-X118R, X009E-X040E-X124I,X009E-X040E-X128S, X009E-X040E-X129P, X009E-X040E-X130S,X009E-X040E-X145R, X009E-X040E-X166Q, X009E-X040E-X185Q,X009E-X040E-X210I, X009E-X040E-X217L, X009E-X040E-X218S,X009E-X040E-X248D, X009E-X040E-X259P, X009E-X069S-X076D,X009E-X069S-X078N, X009E-X069S-X079I, X009E-X069S-X087D,X009E-X069S-X118R, X009E-X069S-X124I, X009E-X069S-X128S,X009E-X069S-X129P, X009E-X069S-X130S, X009E-X069S-X145R,X009E-X069S-X166Q, X009E-X069S-X185Q, X009E-X069S-X210I,X009E-X069S-X217L, X009E-X069S-X218S, X009E-X069S-X248D,X009E-X069S-X259P, X009E-X076D-X078N, X009E-X076D-X079I,X009E-X076D-X087D, X009E-X076D-X118R, X009E-X076D-X124I,X009E-X076D-X128S, X009E-X076D-X129P, X009E-X076D-X130S,X009E-X076D-X145R, X009E-X076D-X166Q, X009E-X076D-X185Q,X009E-X076D-X210I, X009E-X076D-X217L, X009E-X076D-X218S,X009E-X076D-X248D, X009E-X076D-X259P, X009E-X078N-X079I,X009E-X078N-X087D, X009E-X078N-X118R, X009E-X078N-X124I,X009E-X078N-X128S, X009E-X078N-X129P, X009E-X078N-X130S,X009E-X078N-X145R, X009E-X078N-X166Q, X009E-X078N-X185Q,X009E-X078N-X210I, X009E-X078N-X217L, X009E-X078N-X218S,X009E-X078N-X248D, X009E-X078N-X259P, X009E-X079I-X087D,X009E-X079I-X118R, X009E-X079I-X124I, X009E-X079I-X128S,X009E-X079I-X129P, X009E-X079I-X130S, X009E-X079I-X145R,X009E-X079I-X166Q, X009E-X079I-X185Q, X009E-X079I-X210I,X009E-X079I-X217L, X009E-X079I-X218S, X009E-X079I-X248D,X009E-X079I-X259P, X009E-X087D-X118R, X009E-X087D-X124I,X009E-X087D-X128S, X009E-X087D-X129P, X009E-X087D-X130S,X009E-X087D-X145R, X009E-X087D-X166Q, X009E-X087D-X185Q,X009E-X087D-X210I, X009E-X087D-X217L, X009E-X087D-X218S,X009E-X087D-X248D, X009E-X087D-X259P, X009E-X118R-X124I,X009E-X118R-X128S, X009E-X118R-X129P, X009E-X118R-X130S,X009E-X118R-X145R, X009E-X118R-X166Q, X009E-X118R-X185Q,X009E-X118R-X210I, X009E-X118R-X217L, X009E-X118R-X218S,X009E-X118R-X248D, X009E-X118R-X259P, X009E-X124I-X128S,X009E-X124I-X129P, X009E-X124I-X130S, X009E-X124I-X145R,X009E-X124I-X166Q, X009E-X124I-X185Q, X009E-X124I-X210I,X009E-X124I-X217L, X009E-X124I-X218S, X009E-X124I-X248D,X009E-X124I-X259P, X009E-X128S-X129P, X009E-X128S-X130S,X009E-X128S-X145R, X009E-X128S-X166Q, X009E-X128S-X185Q,X009E-X128S-X210I, X009E-X128S-X217L, X009E-X128S-X218S,X009E-X128S-X248D, X009E-X128S-X259P, X009E-X129P-X130S,X009E-X129P-X145R, X009E-X129P-X166Q, X009E-X129P-X185Q,X009E-X129P-X210I, X009E-X129P-X217L, X009E-X129P-X218S,X009E-X129P-X248D, X009E-X129P-X259P, X009E-X130S-X145R,X009E-X130S-X166Q, X009E-X130S-X185Q, X009E-X130S-X210I,X009E-X130S-X217L, X009E-X130S-X218S, X009E-X130S-X248D,X009E-X130S-X259P, X009E-X145R-X166Q, X009E-X145R-X185Q,X009E-X145R-X210I, X009E-X145R-X217L, X009E-X145R-X218S,X009E-X145R-X248D, X009E-X145R-X259P, X009E-X166Q-X185Q,X009E-X166Q-X210I, X009E-X166Q-X217L, X009E-X166Q-X218S,X009E-X166Q-X248D, X009E-X166Q-X259P, X009E-X185Q-X210I,X009E-X185Q-X217L, X009E-X185Q-X218S, X009E-X185Q-X248D,X009E-X185Q-X259P, X009E-X210I-X217L, X009E-X210I-X218S,X009E-X210I-X248D, X009E-X210I-X259P, X009E-X217L-X218S,X009E-X217L-X248D, X009E-X217L-X259P, X009E-X218S-X248D,X009E-X218S-X259P, X009E-X248D-X259P, X024Q-X040E-X069S,X024Q-X040E-X076D, X024Q-X040E-X078N, X024Q-X040E-X079I,X024Q-X040E-X087D, X024Q-X040E-X118R, X024Q-X040E-X124I,X024Q-X040E-X128S, 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X124I-X145R-X259P, X124I-X166Q-X185Q,X124I-X166Q-X210I, X124I-X166Q-X217L, X124I-X166Q-X218S,X124I-X166Q-X248D, X124I-X166Q-X259P, X124I-X185Q-X210I,X124I-X185Q-X217L, X124I-X185Q-X218S, X124I-X185Q-X248D,X124I-X185Q-X259P, X124I-X210I-X217L, X124I-X210I-X218S,X124I-X210I-X248D, X124I-X210I-X259P, X124I-X217L-X218S,X124I-X217L-X248D, X124I-X217L-X259P, X124I-X218S-X248D,X124I-X218S-X259P, X124I-X248D-X259P, X128S-X129P-X130S,X128S-X129P-X145R, X128S-X129P-X166Q, X128S-X129P-X185Q,X128S-X129P-X210I, X128S-X129P-X217L, X128S-X129P-X218S,X128S-X129P-X248D, X128S-X129P-X259P, X128S-X130S-X145R,X128S-X130S-X166Q, X128S-X130S-X185Q, X128S-X130S-X210I,X128S-X130S-X217L, X128S-X130S-X218S, X128S-X130S-X248D,X128S-X130S-X259P, X128S-X145R-X166Q, X128S-X145R-X185Q,X128S-X145R-X210I, X128S-X145R-X217L, X128S-X145R-X218S,X128S-X145R-X248D, X128S-X145R-X259P, X128S-X166Q-X185Q,X128S-X166Q-X210I, X128S-X166Q-X217L, X128S-X166Q-X218S,X128S-X166Q-X248D, X128S-X166Q-X259P, X128S-X185Q-X210I,X128S-X185Q-X217L, X128S-X185Q-X218S, X128S-X185Q-X248D,X128S-X185Q-X259P, X128S-X210I-X217L, X128S-X210I-X218S,X128S-X210I-X248D, X128S-X210I-X259P, X128S-X217L-X218S,X128S-X217L-X248D, X128S-X217L-X259P, X128S-X218S-X248D,X128S-X218S-X259P, X128S-X248D-X259P, X129P-X130S-X145R,X129P-X130S-X166Q, X129P-X130S-X185Q, X129P-X130S-X210I,X129P-X130S-X217L, X129P-X130S-X218S, X129P-X130S-X248D,X129P-X130S-X259P, X129P-X145R-X166Q, X129P-X145R-X185Q,X129P-X145R-X210I, X129P-X145R-X217L, X129P-X145R-X218S,X129P-X145R-X248D, X129P-X145R-X259P, X129P-X166Q-X185Q,X129P-X166Q-X210I, X129P-X166Q-X217L, X129P-X166Q-X218S,X129P-X166Q-X248D, X129P-X166Q-X259P, X129P-X185Q-X210I,X129P-X185Q-X217L, X129P-X185Q-X218S, X129P-X185Q-X248D,X129P-X185Q-X259P, X129P-X210I-X217L, X129P-X210I-X218S,X129P-X210I-X248D, X129P-X210I-X259P, X129P-X217L-X218S,X129P-X217L-X248D, X129P-X217L-X259P, X129P-X218S-X248D,X129P-X218S-X259P, X129P-X248D-X259P, X130S-X145R-X166Q,X130S-X145R-X185Q, X130S-X145R-X210I, X130S-X145R-X217L,X130S-X145R-X218S, X130S-X145R-X248D, X130S-X145R-X259P,X130S-X166Q-X185Q, X130S-X166Q-X210I, X130S-X166Q-X217L,X130S-X166Q-X218S, X130S-X166Q-X248D, X130S-X166Q-X259P,X130S-X185Q-X210I, X130S-X185Q-X217L, X130S-X185Q-X218S,X130S-X185Q-X248D, X130S-X185Q-X259P, X130S-X210I-X217L,X130S-X210I-X218S, X130S-X210I-X248D, X130S-X210I-X259P,X130S-X217L-X218S, X130S-X217L-X248D, X130S-X217L-X259P,X130S-X218S-X248D, X130S-X218S-X259P, X130S-X248D-X259P,X145R-X166Q-X185Q, X145R-X166Q-X210I, X145R-X166Q-X217L,X145R-X166Q-X218S, X145R-X166Q-X248D, X145R-X166Q-X259P,X145R-X185Q-X210I, X145R-X185Q-X217L, X145R-X185Q-X218S,X145R-X185Q-X248D, X145R-X185Q-X259P, X145R-X210I-X217L,X145R-X210I-X218S, X145R-X210I-X248D, X145R-X210I-X259P,X145R-X217L-X218S, X145R-X217L-X248D, X145R-X217L-X259P,X145R-X218S-X248D, X145R-X218S-X259P, X145R-X248D-X259P,X166Q-X185Q-X210I, X166Q-X185Q-X217L, X166Q-X185Q-X218S,X166Q-X185Q-X248D, X166Q-X185Q-X259P, X166Q-X210I-X217L,X166Q-X210I-X218S, X166Q-X210I-X248D, X166Q-X210I-X259P,X166Q-X217L-X218S, X166Q-X217L-X248D, X166Q-X217L-X259P,X166Q-X218S-X248D, X166Q-X218S-X259P, X166Q-X248D-X259P,X185Q-X210I-X217L, X185Q-X210I-X218S, X185Q-X210I-X248D,X185Q-X210I-X259P, X185Q-X217L-X218S, X185Q-X217L-X248D,X185Q-X217L-X259P, X185Q-X218S-X248D, X185Q-X218S-X259P,X185Q-X248D-X259P, X210I-X217L-X218S, X210I-X217L-X248D,X210I-X217L-X259P, X210I-X218S-X248D, X210I-X218S-X259P,X210I-X248D-X259P, X217L-X218S-X248D, X217L-X218S-X259P,X217L-X248D-X259P, X218S-X248D-X259P, where the positions are numberedby correspondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In other embodiments, the subtilisin variants disclosed herein contain acombination of three or more features with respect to SEQ ID NO: 1,where the combination of three or more features are selected from thegroup consisting of X003V-X009E-X040E, X003V-X009E-X069S,X003V-X009E-X076D, X003V-X009E-X078N, X003V-X009E-X166Q,X003V-X009E-X185Q, X003V-X009E-X218S, X003V-X009E-X259P,X003V-X040E-X069S, X003V-X040E-X076D, X003V-X040E-X078N,X003V-X040E-X166Q, X003V-X040E-X185Q, X003V-X040E-X218S,X003V-X040E-X259P, X003V-X069S-X076D, X003V-X069S-X078N,X003V-X069S-X128S, X003V-X069S-X129P, X003V-X069S-X166Q,X003V-X069S-X185Q, X003V-X069S-X218S, X003V-X069S-X259P,X003V-X076D-X078N, X003V-X076D-X129P, X003V-X076D-X166Q,X003V-X076D-X185Q, X003V-X076D-X218S, X003V-X076D-X259P,X003V-X078N-X128S, X003V-X078N-X166Q, X003V-X078N-X185Q,X003V-X078N-X218S, X003V-X078N-X259P, X003V-X124I-X128S,X003V-X124I-X259P, X003V-X128S-X166Q, X003V-X128S-X259P,X003V-X129P-X166Q, X003V-X129P-X185Q, X003V-X129P-X259P,X003V-X166Q-X185Q, X003V-X166Q-X218S, X003V-X166Q-X259P,X003V-X185Q-X218S, X003V-X185Q-X259P, X003V-X218S-X259P,X009E-X040E-X069S, X009E-X040E-X076D, X009E-X040E-X078N,X009E-X040E-X166Q, X009E-X040E-X185Q, X009E-X040E-X218S,X009E-X040E-X259P, X009E-X069S-X076D, X009E-X069S-X078N,X009E-X069S-X166Q, X009E-X069S-X185Q, X009E-X069S-X218S,X009E-X069S-X259P, X009E-X076D-X078N, X009E-X076D-X166Q,X009E-X076D-X185Q, X009E-X076D-X218S, X009E-X076D-X259P,X009E-X078N-X166Q, X009E-X078N-X185Q, X009E-X078N-X218S,X009E-X078N-X259P, X009E-X166Q-X185Q, X009E-X166Q-X218S,X009E-X166Q-X259P, X009E-X185Q-X218S, X009E-X185Q-X259P,X009E-X218S-X259P, X040E-X069S-X076D, X040E-X069S-X078N,X040E-X069S-X166Q, X040E-X069S-X185Q, X040E-X069S-X218S,X040E-X069S-X259P, X040E-X076D-X078N, X040E-X076D-X166Q,X040E-X076D-X185Q, X040E-X076D-X218S, X040E-X076D-X259P,X040E-X078N-X129P, X040E-X078N-X166Q, X040E-X078N-X185Q,X040E-X078N-X218S, X040E-X078N-X259P, X040E-X166Q-X185Q,X040E-X166Q-X218S, X040E-X166Q-X259P, X040E-X185Q-X218S,X040E-X185Q-X259P, X040E-X218S-X259P, X069S-X076D-X078N,X069S-X076D-X128S, X069S-X076D-X166Q, X069S-X076D-X185Q,X069S-X076D-X218S, X069S-X076D-X259P, X069S-X078N-X124I,X069S-X078N-X166Q, X069S-X078N-X185Q, X069S-X078N-X218S,X069S-X078N-X259P, X069S-X128S-X185Q, X069S-X129P-X166Q,X069S-X129P-X185Q, X069S-X129P-X218S, X069S-X129P-X259P,X069S-X166Q-X185Q, X069S-X166Q-X218S, X069S-X166Q-X259P,X069S-X185Q-X218S, X069S-X185Q-X259P, X069S-X218S-X259P,X076D-X078N-X166Q, X076D-X078N-X185Q, X076D-X078N-X218S,X076D-X078N-X259P, X076D-X128S-X166Q, X076D-X129P-X218S,X076D-X166Q-X185Q, X076D-X166Q-X218S, X076D-X166Q-X259P,X076D-X185Q-X218S, X076D-X185Q-X259P, X076D-X218S-X259P,X078N-X124I-X166Q, X078N-X128S-X166Q, X078N-X129P-X259P,X078N-X166Q-X185Q, X078N-X166Q-X218S, X078N-X166Q-X259P,X078N-X185Q-X218S, X078N-X185Q-X259P, X078N-X218S-X259P,X124I-X128S-X166Q, X124I-X128S-X185Q, X124I-X129P-X185Q,X124I-X129P-X259P, X124I-X166Q-X259P, X124I-X185Q-X259P,X124I-X218S-X259P, X128S-X129P-X218S, X128S-X166Q-X185Q,X128S-X166Q-X259P, X128S-X185Q-X218S, X128S-X185Q-X259P,X166Q-X185Q-X218S, X166Q-X185Q-X259P, X166Q-X218S-X259P, andX185Q-X218S-X259P, where the positions are numbered by correspondencewith the amino acid sequence of SEQ ID NO:1 (BPN′).

In other embodiments, the subtilisin variants disclosed herein contain acombination of four or more features with respect to SEQ ID NO: 1, wherethe combination of four or more features are selected from the groupconsisting of X003V-X009E-X024Q-X040E, X003V-X009E-X024Q-X069S,X003V-X009E-X024Q-X076D, X003V-X009E-X024Q-X078N,X003V-X009E-X024Q-X079I, X003V-X009E-X024Q-X087D,X003V-X009E-X024Q-X118R, X003V-X009E-X024Q-X124I,X003V-X009E-X024Q-X128S, X003V-X009E-X024Q-X129P,X003V-X009E-X024Q-X130S, X003V-X009E-X024Q-X145R,X003V-X009E-X024Q-X166Q, X003V-X009E-X024Q-X185Q,X003V-X009E-X024Q-X210I, X003V-X009E-X024Q-X217L,X003V-X009E-X024Q-X218S, X003V-X009E-X024Q-X248D,X003V-X009E-X024Q-X259P, X003V-X009E-X040E-X069S,X003V-X009E-X040E-X076D, X003V-X009E-X040E-X078N,X003V-X009E-X040E-X079I, X003V-X009E-X040E-X087D,X003V-X009E-X040E-X118R, X003V-X009E-X040E-X124I,X003V-X009E-X040E-X128S, X003V-X009E-X040E-X129P,X003V-X009E-X040E-X130S, X003V-X009E-X040E-X145R,X003V-X009E-X040E-X166Q, X003V-X009E-X040E-X185Q,X003V-X009E-X040E-X210I, X003V-X009E-X040E-X217L,X003V-X009E-X040E-X218S, X003V-X009E-X040E-X248D,X003V-X009E-X040E-X259P, X003V-X009E-X069S-X076D,X003V-X009E-X069S-X078N, X003V-X009E-X069S-X079I,X003V-X009E-X069S-X087D, X003V-X009E-X069S-X118R,X003V-X009E-X069S-X124I, X003V-X009E-X069S-X128S,X003V-X009E-X069S-X129P, X003V-X009E-X069S-X130S,X003V-X009E-X069S-X145R, X003V-X009E-X069S-X166Q,X003V-X009E-X069S-X185Q, X003V-X009E-X069S-X210I,X003V-X009E-X069S-X217L, X003V-X009E-X069S-X218S,X003V-X009E-X069S-X248D, X003V-X009E-X069S-X259P,X003V-X009E-X076D-X078N, X003V-X009E-X076D-X079I,X003V-X009E-X076D-X087D, X003V-X009E-X076D-X118R,X003V-X009E-X076D-X124I, X003V-X009E-X076D-X128S,X003V-X009E-X076D-X129P, X003V-X009E-X076D-X130S,X003V-X009E-X076D-X145R, X003V-X009E-X076D-X166Q,X003V-X009E-X076D-X185Q, X003V-X009E-X076D-X210I,X003V-X009E-X076D-X217L, X003V-X009E-X076D-X218S,X003V-X009E-X076D-X248D, X003V-X009E-X076D-X259P,X003V-X009E-X078N-X079I, X003V-X009E-X078N-X087D,X003V-X009E-X078N-X118R, X003V-X009E-X078N-X124I,X003V-X009E-X078N-X128S, X003V-X009E-X078N-X129P,X003V-X009E-X078N-X130S, X003V-X009E-X078N-X145R,X003V-X009E-X078N-X166Q, X003V-X009E-X078N-X185Q,X003V-X009E-X078N-X210I, X003V-X009E-X078N-X217L,X003V-X009E-X078N-X218S, X003V-X009E-X078N-X248D,X003V-X009E-X078N-X259P, X003V-X009E-X079I-X087D,X003V-X009E-X079I-X118R, X003V-X009E-X079I-X124I,X003V-X009E-X079I-X128S, X003V-X009E-X079I-X129P,X003V-X009E-X079I-X130S, X003V-X009E-X079I-X145R,X003V-X009E-X079I-X166Q, X003V-X009E-X079I-X185Q,X003V-X009E-X079I-X210I, X003V-X009E-X079I-X217L,X003V-X009E-X079I-X218S, X003V-X009E-X079I-X248D,X003V-X009E-X079I-X259P, X003V-X009E-X087D-X118R,X003V-X009E-X087D-X124I, X003V-X009E-X087D-X128S,X003V-X009E-X087D-X129P, X003V-X009E-X087D-X130S,X003V-X009E-X087D-X145R, X003V-X009E-X087D-X166Q,X003V-X009E-X087D-X185Q, X003V-X009E-X087D-X210I,X003V-X009E-X087D-X217L, X003V-X009E-X087D-X218S,X003V-X009E-X087D-X248D, X003V-X009E-X087D-X259P,X003V-X009E-X118R-X124I, X003V-X009E-X118R-X128S,X003V-X009E-X118R-X129P, X003V-X009E-X118R-X130S,X003V-X009E-X118R-X145R, X003V-X009E-X118R-X166Q,X003V-X009E-X118R-X185Q, X003V-X009E-X118R-X210I,X003V-X009E-X118R-X217L, X003V-X009E-X118R-X218S,X003V-X009E-X118R-X248D, X003V-X009E-X118R-X259P,X003V-X009E-X124I-X128S, X003V-X009E-X124I-X129P,X003V-X009E-X124I-X130S, X003V-X009E-X124I-X145R,X003V-X009E-X124I-X166Q, X003V-X009E-X124I-X185Q,X003V-X009E-X124I-X210I, X003V-X009E-X124I-X217L,X003V-X009E-X124I-X218S, X003V-X009E-X124I-X248D,X003V-X009E-X124I-X259P, X003V-X009E-X128 S-X129P, X003V-X009E-X128S-X130S, X003V-X009E-X128 S-X145R, X003V-X009E-X128 S-X166Q,X003V-X009E-X128 S-X185Q, X003V-X009E-X128 S-X210I,X003V-X009E-X128S-X217L, X003V-X009E-X128S-X218S,X003V-X009E-X128S-X248D, X003V-X009E-X128S-X259P,X003V-X009E-X129P-X130S, X003V-X009E-X129P-X145R,X003V-X009E-X129P-X166Q, X003V-X009E-X129P-X185Q,X003V-X009E-X129P-X210I, X003V-X009E-X129P-X217L,X003V-X009E-X129P-X218S, X003V-X009E-X129P-X248D,X003V-X009E-X129P-X259P, X003V-X009E-X130S-X145R,X003V-X009E-X130S-X166Q, X003V-X009E-X130S-X185Q,X003V-X009E-X130S-X210I, X003V-X009E-X130S-X217L,X003V-X009E-X130S-X218S, X003V-X009E-X130S-X248D,X003V-X009E-X130S-X259P, X003V-X009E-X145R-X166Q,X003V-X009E-X145R-X185Q, X003V-X009E-X145R-X210I,X003V-X009E-X145R-X217L, X003V-X009E-X145R-X218S,X003V-X009E-X145R-X248D, X003V-X009E-X145R-X259P,X003V-X009E-X166Q-X185Q, X003V-X009E-X166Q-X210I,X003V-X009E-X166Q-X217L, X003V-X009E-X166Q-X218S,X003V-X009E-X166Q-X248D, X003V-X009E-X166Q-X259P,X003V-X009E-X185Q-X210I, X003V-X009E-X185Q-X217L,X003V-X009E-X185Q-X218S, X003V-X009E-X185Q-X248D,X003V-X009E-X185Q-X259P, X003V-X009E-X210I-X217L,X003V-X009E-X210I-X218S, X003V-X009E-X210I-X248D,X003V-X009E-X210I-X259P, X003V-X009E-X217L-X218S,X003V-X009E-X217L-X248D, X003V-X009E-X217L-X259P,X003V-X009E-X218S-X248D, X003V-X009E-X218S-X259P,X003V-X009E-X248D-X259P, X003V-X024Q-X040E-X069S,X003V-X024Q-X040E-X076D, X003V-X024Q-X040E-X078N,X003V-X024Q-X040E-X079I, X003V-X024Q-X040E-X087D,X003V-X024Q-X040E-X118R, X003V-X024Q-X040E-X124I,X003V-X024Q-X040E-X128S, X003V-X024Q-X040E-X129P,X003V-X024Q-X040E-X130S, X003V-X024Q-X040E-X145R,X003V-X024Q-X040E-X166Q, X003V-X024Q-X040E-X185Q,X003V-X024Q-X040E-X210I, X003V-X024Q-X040E-X217L,X003V-X024Q-X040E-X218S, X003V-X024Q-X040E-X248D,X003V-X024Q-X040E-X259P, X003V-X024Q-X069S-X076D,X003V-X024Q-X069S-X078N, X003V-X024Q-X069S-X079I,X003V-X024Q-X069S-X087D, X003V-X024Q-X069S-X118R,X003V-X024Q-X069S-X124I, X003V-X024Q-X069S-X128S,X003V-X024Q-X069S-X129P, X003V-X024Q-X069S-X130S,X003V-X024Q-X069S-X145R, X003V-X024Q-X069S-X166Q,X003V-X024Q-X069S-X185Q, X003V-X024Q-X069S-X210I,X003V-X024Q-X069S-X217L, X003V-X024Q-X069S-X218S,X003V-X024Q-X069S-X248D, X003V-X024Q-X069S-X259P,X003V-X024Q-X076D-X078N, X003V-X024Q-X076D-X079I,X003V-X024Q-X076D-X087D, X003V-X024Q-X076D-X118R,X003V-X024Q-X076D-X124I, 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X128S-X130S-X166Q-X210I,X128S-X130S-X166Q-X217L, X128S-X130S-X166Q-X218S,X128S-X130S-X166Q-X248D, X128S-X130S-X166Q-X259P,X128S-X130S-X185Q-X210I, X128S-X130S-X185Q-X217L,X128S-X130S-X185Q-X218S, X128S-X130S-X185Q-X248D,X128S-X130S-X185Q-X259P, X128S-X130S-X210I-X217L,X128S-X130S-X210I-X218S, X128S-X130S-X210I-X248D,X128S-X130S-X210I-X259P, X128S-X130S-X217L-X218S,X128S-X130S-X217L-X248D, X128S-X130S-X217L-X259P,X128S-X130S-X218S-X248D, X128S-X130S-X218S-X259P,X128S-X130S-X248D-X259P, X128S-X145R-X166Q-X185Q,X128S-X145R-X166Q-X210I, X128S-X145R-X166Q-X217L,X128S-X145R-X166Q-X218S, X128S-X145R-X166Q-X248D,X128S-X145R-X166Q-X259P, X128S-X145R-X185Q-X210I,X128S-X145R-X185Q-X217L, X128S-X145R-X185Q-X218S,X128S-X145R-X185Q-X248D, X128S-X145R-X185Q-X259P,X128S-X145R-X210I-X217L, X128S-X145R-X210I-X218S,X128S-X145R-X210I-X248D, X128S-X145R-X210I-X259P,X128S-X145R-X217L-X218S, X128S-X145R-X217L-X248D,X128S-X145R-X217L-X259P, X128S-X145R-X218S-X248D,X128S-X145R-X218S-X259P, X128S-X145R-X248D-X259P,X128S-X166Q-X185Q-X210I, X128S-X166Q-X185Q-X217L,X128S-X166Q-X185Q-X218S, X128S-X166Q-X185Q-X248D,X128S-X166Q-X185Q-X259P, X128S-X166Q-X210I-X217L,X128S-X166Q-X210I-X218S, X128S-X166Q-X210I-X248D,X128S-X166Q-X210I-X259P, X128S-X166Q-X217L-X218S,X128S-X166Q-X217L-X248D, X128S-X166Q-X217L-X259P,X128S-X166Q-X218S-X248D, X128S-X166Q-X218S-X259P,X128S-X166Q-X248D-X259P, X128S-X185Q-X210I-X217L,X128S-X185Q-X210I-X218S, X128S-X185Q-X210I-X248D,X128S-X185Q-X210I-X259P, X128S-X185Q-X217L-X218S,X128S-X185Q-X217L-X248D, X128S-X185Q-X217L-X259P,X128S-X185Q-X218S-X248D, X128S-X185Q-X218S-X259P,X128S-X185Q-X248D-X259P, X128S-X210I-X217L-X218S,X128S-X210I-X217L-X248D, X128S-X210I-X217L-X259P,X128S-X210I-X218S-X248D, X128S-X210I-X218S-X259P,X128S-X210I-X248D-X259P, X128S-X217L-X218S-X248D,X128S-X217L-X218S-X259P, X128S-X217L-X248D-X259P,X128S-X218S-X248D-X259P, X129P-X130S-X145R-X166Q,X129P-X130S-X145R-X185Q, X129P-X130S-X145R-X210I,X129P-X130S-X145R-X217L, X129P-X130S-X145R-X218S,X129P-X130S-X145R-X248D, X129P-X130S-X145R-X259P,X129P-X130S-X166Q-X185Q, X129P-X130S-X166Q-X210I,X129P-X130S-X166Q-X217L, X129P-X130S-X166Q-X218S,X129P-X130S-X166Q-X248D, X129P-X130S-X166Q-X259P,X129P-X130S-X185Q-X210I, X129P-X130S-X185Q-X217L,X129P-X130S-X185Q-X218S, X129P-X130S-X185Q-X248D,X129P-X130S-X185Q-X259P, X129P-X130S-X210I-X217L,X129P-X130S-X210I-X218S, X129P-X130S-X210I-X248D,X129P-X130S-X210I-X259P, X129P-X130S-X217L-X218S,X129P-X130S-X217L-X248D, X129P-X130S-X217L-X259P,X129P-X130S-X218S-X248D, X129P-X130S-X218S-X259P,X129P-X130S-X248D-X259P, X129P-X145R-X166Q-X185Q,X129P-X145R-X166Q-X210I, X129P-X145R-X166Q-X217L,X129P-X145R-X166Q-X218S, X129P-X145R-X166Q-X248D,X129P-X145R-X166Q-X259P, X129P-X145R-X185Q-X210I,X129P-X145R-X185Q-X217L, X129P-X145R-X185Q-X218S,X129P-X145R-X185Q-X248D, X129P-X145R-X185Q-X259P,X129P-X145R-X210I-X217L, X129P-X145R-X210I-X218S,X129P-X145R-X210I-X248D, X129P-X145R-X210I-X259P,X129P-X145R-X217L-X218S, X129P-X145R-X217L-X248D,X129P-X145R-X217L-X259P, X129P-X145R-X218S-X248D,X129P-X145R-X218S-X259P, X129P-X145R-X248D-X259P,X129P-X166Q-X185Q-X210I, X129P-X166Q-X185Q-X217L,X129P-X166Q-X185Q-X218S, X129P-X166Q-X185Q-X248D,X129P-X166Q-X185Q-X259P, X129P-X166Q-X210I-X217L,X129P-X166Q-X210I-X218S, X129P-X166Q-X210I-X248D,X129P-X166Q-X210I-X259P, X129P-X166Q-X217L-X218S,X129P-X166Q-X217L-X248D, X129P-X166Q-X217L-X259P,X129P-X166Q-X218S-X248D, X129P-X166Q-X218S-X259P,X129P-X166Q-X248D-X259P, X129P-X185Q-X210I-X217L,X129P-X185Q-X210I-X218S, X129P-X185Q-X210I-X248D,X129P-X185Q-X210I-X259P, X129P-X185Q-X217L-X218S,X129P-X185Q-X217L-X248D, X129P-X185Q-X217L-X259P,X129P-X185Q-X218S-X248D, X129P-X185Q-X218S-X259P,X129P-X185Q-X248D-X259P, X129P-X210I-X217L-X218S,X129P-X210I-X217L-X248D, X129P-X210I-X217L-X259P,X129P-X210I-X218S-X248D, X129P-X210I-X218S-X259P,X129P-X210I-X248D-X259P, X129P-X217L-X218S-X248D,X129P-X217L-X218S-X259P, X129P-X217L-X248D-X259P,X129P-X218S-X248D-X259P, X130S-X145R-X166Q-X185Q,X130S-X145R-X166Q-X210I, X130S-X145R-X166Q-X217L,X130S-X145R-X166Q-X218S, X130S-X145R-X166Q-X248D,X130S-X145R-X166Q-X259P, X130S-X145R-X185Q-X210I,X130S-X145R-X185Q-X217L, X130S-X145R-X185Q-X218S,X130S-X145R-X185Q-X248D, X130S-X145R-X185Q-X259P,X130S-X145R-X210I-X217L, X130S-X145R-X210I-X218S,X130S-X145R-X210I-X248D, X130S-X145R-X210I-X259P,X130S-X145R-X217L-X218S, X130S-X145R-X217L-X248D,X130S-X145R-X217L-X259P, X130S-X145R-X218S-X248D,X130S-X145R-X218S-X259P, X130S-X145R-X248D-X259P,X130S-X166Q-X185Q-X210I, X130S-X166Q-X185Q-X217L,X130S-X166Q-X185Q-X218S, X130S-X166Q-X185Q-X248D,X130S-X166Q-X185Q-X259P, X130S-X166Q-X210I-X217L,X130S-X166Q-X210I-X218S, X130S-X166Q-X210I-X248D,X130S-X166Q-X210I-X259P, X130S-X166Q-X217L-X218S,X130S-X166Q-X217L-X248D, X130S-X166Q-X217L-X259P,X130S-X166Q-X218S-X248D, X130S-X166Q-X218S-X259P,X130S-X166Q-X248D-X259P, X130S-X185Q-X210I-X217L,X130S-X185Q-X210I-X218S, X130S-X185Q-X210I-X248D,X130S-X185Q-X210I-X259P, X130S-X185Q-X217L-X218S,X130S-X185Q-X217L-X248D, X130S-X185Q-X217L-X259P,X130S-X185Q-X218S-X248D, X130S-X185Q-X218S-X259P,X130S-X185Q-X248D-X259P, X130S-X210I-X217L-X218S,X130S-X210I-X217L-X248D, X130S-X210I-X217L-X259P,X130S-X210I-X218S-X248D, X130S-X210I-X218S-X259P,X130S-X210I-X248D-X259P, X130S-X217L-X218S-X248D,X130S-X217L-X218S-X259P, X130S-X217L-X248D-X259P,X130S-X218S-X248D-X259P, X145R-X166Q-X185Q-X210I,X145R-X166Q-X185Q-X217L, X145R-X166Q-X185Q-X218S,X145R-X166Q-X185Q-X248D, X145R-X166Q-X185Q-X259P,X145R-X166Q-X210I-X217L, X145R-X166Q-X210I-X218S,X145R-X166Q-X210I-X248D, X145R-X166Q-X210I-X259P,X145R-X166Q-X217L-X218S, X145R-X166Q-X217L-X248D,X145R-X166Q-X217L-X259P, X145R-X166Q-X218S-X248D,X145R-X166Q-X218S-X259P, X145R-X166Q-X248D-X259P,X145R-X185Q-X210I-X217L, X145R-X185Q-X210I-X218S,X145R-X185Q-X210I-X248D, X145R-X185Q-X210I-X259P,X145R-X185Q-X217L-X218S, X145R-X185Q-X217L-X248D,X145R-X185Q-X217L-X259P, X145R-X185Q-X218S-X248D,X145R-X185Q-X218S-X259P, X145R-X185Q-X248D-X259P,X145R-X210I-X217L-X218S, X145R-X210I-X217L-X248D,X145R-X210I-X217L-X259P, X145R-X210I-X218S-X248D,X145R-X210I-X218S-X259P, X145R-X210I-X248D-X259P,X145R-X217L-X218S-X248D, X145R-X217L-X218S-X259P,X145R-X217L-X248D-X259P, X145R-X218S-X248D-X259P,X166Q-X185Q-X210I-X217L, X166Q-X185Q-X210I-X218S,X166Q-X185Q-X210I-X248D, X166Q-X185Q-X210I-X259P,X166Q-X185Q-X217L-X218S, X166Q-X185Q-X217L-X248D,X166Q-X185Q-X217L-X259P, X166Q-X185Q-X218S-X248D,X166Q-X185Q-X218S-X259P, X166Q-X185Q-X248D-X259P,X166Q-X210I-X217L-X218S, X166Q-X210I-X217L-X248D,X166Q-X210I-X217L-X259P, X166Q-X210I-X218S-X248D,X166Q-X210I-X218S-X259P, X166Q-X210I-X248D-X259P,X166Q-X217L-X218S-X248D, X166Q-X217L-X218S-X259P,X166Q-X217L-X248D-X259P, X166Q-X218S-X248D-X259P,X185Q-X210I-X217L-X218S, X185Q-X210I-X217L-X248D,X185Q-X210I-X217L-X259P, X185Q-X210I-X218S-X248D,X185Q-X210I-X218S-X259P, X185Q-X210I-X248D-X259P,X185Q-X217L-X218S-X248D, X185Q-X217L-X218S-X259P,X185Q-X217L-X248D-X259P, X185Q-X218S-X248D-X259P,X210I-X217L-X218S-X248D, X210I-X217L-X218S-X259P,X210I-X217L-X248D-X259P, X210I-X218S-X248D-X259P,X217L-X218S-X248D-X259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In other embodiments, the subtilisin variants disclosed herein contain acombination of four or more features with respect to SEQ ID NO: 1, wherethe combination of four or more features are selected from the groupconsisting of X003V-X009E-X040E-X076D, X003V-X009E-X040E-X166Q,X003V-X009E-X040E-X185Q, X003V-X009E-X069S-X078N,X003V-X009E-X069S-X166Q, X003V-X009E-X069S-X185Q,X003V-X009E-X076D-X166Q, X003V-X009E-X076D-X218S,X003V-X009E-X166Q-X185Q, X003V-X009E-X166Q-X259P,X003V-X009E-X218S-X259P, X003V-X040E-X069S-X076D,X003V-X040E-X069S-X166Q, X003V-X040E-X076D-X078N,X003V-X040E-X076D-X129P, X003V-X040E-X076D-X185Q,X003V-X040E-X076D-X218S, X003V-X040E-X078N-X124I,X003V-X040E-X124I-X218S, X003V-X040E-X166Q-X185Q,X003V-X040E-X166Q-X259P, X003V-X069S-X076D-X078N,X003V-X069S-X076D-X128S, X003V-X069S-X076D-X185Q,X003V-X069S-X076D-X218S, X003V-X069S-X076D-X259P,X003V-X069S-X078N-X128S, X003V-X069S-X078N-X129P,X003V-X069S-X078N-X166Q, X003V-X069S-X078N-X185Q,X003V-X069S-X078N-X218S, X003V-X069S-X078N-X259P,X003V-X069S-X124I-X218S, X003V-X069S-X128S-X166Q,X003V-X069S-X128S-X185Q, X003V-X069S-X128S-X259P,X003V-X069S-X129P-X185Q, X003V-X069S-X129P-X218S,X003V-X069S-X129P-X259P, X003V-X069S-X166Q-X185Q,X003V-X069S-X166Q-X218S, X003V-X069S-X185Q-X218S,X003V-X069S-X185Q-X259P, X003V-X069S-X218S-X259P,X003V-X076D-X078N-X128S, X003V-X076D-X078N-X166Q,X003V-X076D-X078N-X259P, X003V-X076D-X124I-X166Q,X003V-X076D-X128S-X259P, X003V-X076D-X129P-X166Q,X003V-X076D-X129P-X185Q, X003V-X076D-X129P-X259P,X003V-X076D-X166Q-X185Q, X003V-X076D-X166Q-X259P,X003V-X076D-X185Q-X259P, X003V-X076D-X218S-X259P,X003V-X078N-X124I-X166Q, X003V-X078N-X128S-X185Q,X003V-X078N-X128S-X218S, X003V-X078N-X129P-X185Q,X003V-X078N-X129P-X259P, X003V-X078N-X166Q-X259P,X003V-X078N-X185Q-X218S, X003V-X078N-X185Q-X259P,X003V-X078N-X218S-X259P, X003V-X124I-X128S-X166Q,X003V-X124I-X128S-X218S, X003V-X124I-X128S-X259P,X003V-X124I-X166Q-X259P, X003V-X124I-X185Q-X259P,X003V-X128S-X129P-X185Q, X003V-X128S-X166Q-X218S,X003V-X128S-X185Q-X218S, X003V-X128S-X185Q-X259P,X003V-X128S-X218S-X259P, X003V-X129P-X185Q-X218S,X003V-X166Q-X185Q-X218S, X003V-X166Q-X185Q-X259P,X003V-X166Q-X218S-X259P, X003V-X185Q-X218S-X259P,X009E-X040E-X069S-X076D, X009E-X040E-X069S-X078N,X009E-X040E-X069S-X185Q, X009E-X040E-X069S-X218S,X009E-X040E-X069S-X259P, X009E-X040E-X076D-X078N,X009E-X040E-X076D-X185Q, X009E-X040E-X078N-X185Q,X009E-X040E-X078N-X259P, X009E-X040E-X166Q-X218S,X009E-X040E-X166Q-X259P, X009E-X040E-X185Q-X218S,X009E-X040E-X185Q-X259P, X009E-X040E-X218S-X259P,X009E-X069S-X076D-X078N, X009E-X069S-X076D-X166Q,X009E-X069S-X076D-X185Q, X009E-X069S-X076D-X218S,X009E-X069S-X076D-X259P, X009E-X069S-X078N-X166Q,X009E-X069S-X078N-X218S, X009E-X069S-X166Q-X185Q,X009E-X069S-X166Q-X218S, X009E-X069S-X166Q-X259P,X009E-X069S-X185Q-X218S, X009E-X069S-X218S-X259P,X009E-X076D-X078N-X166Q, X009E-X076D-X078N-X185Q,X009E-X076D-X078N-X259P, X009E-X076D-X166Q-X185Q,X009E-X076D-X166Q-X218S, X009E-X076D-X166Q-X259P,X009E-X076D-X185Q-X218S, X009E-X076D-X185Q-X259P,X009E-X076D-X218S-X259P, X009E-X078N-X166Q-X185Q,X009E-X078N-X166Q-X218S, X009E-X078N-X185Q-X218S,X009E-X078N-X185Q-X259P, X009E-X078N-X218S-X259P,X009E-X166Q-X185Q-X218S, X009E-X166Q-X185Q-X259P,X009E-X166Q-X218S-X259P, X009E-X185Q-X218S-X259P,X040E-X069S-X076D-X078N, X040E-X069S-X076D-X185Q,X040E-X069S-X078N-X166Q, X040E-X069S-X078N-X218S,X040E-X069S-X078N-X259P, X040E-X069S-X129P-X218S,X040E-X069S-X166Q-X218S, X040E-X069S-X166Q-X259P,X040E-X069S-X185Q-X218S, X040E-X069S-X185Q-X259P,X040E-X069S-X218S-X259P, X040E-X076D-X078N-X166Q,X040E-X076D-X078N-X185Q, X040E-X076D-X078N-X218S,X040E-X076D-X124I-X218S, X040E-X076D-X166Q-X185Q,X040E-X076D-X166Q-X218S, X040E-X076D-X166Q-X259P,X040E-X076D-X185Q-X218S, X040E-X076D-X185Q-X259P,X040E-X076D-X218S-X259P, X040E-X078N-X166Q-X218S,X040E-X078N-X185Q-X259P, X040E-X078N-X218S-X259P,X040E-X124I-X218S-X259P, X040E-X166Q-X185Q-X218S,X040E-X185Q-X218S-X259P, X069S-X076D-X078N-X128S,X069S-X076D-X078N-X185Q, X069S-X076D-X078N-X218S,X069S-X076D-X078N-X259P, X069S-X076D-X124I-X128S,X069S-X076D-X129P-X166Q, X069S-X076D-X129P-X259P,X069S-X076D-X166Q-X185Q, X069S-X076D-X166Q-X218S,X069S-X076D-X166Q-X259P, X069S-X076D-X185Q-X218S,X069S-X076D-X185Q-X259P, X069S-X076D-X218S-X259P,X069S-X078N-X128S-X218S, X069S-X078N-X129P-X185Q,X069S-X078N-X166Q-X185Q, X069S-X078N-X166Q-X218S,X069S-X078N-X185Q-X218S, X069S-X078N-X185Q-X259P,X069S-X078N-X218S-X259P, X069S-X124I-X128S-X185Q,X069S-X124I-X128S-X218S, X069S-X124I-X129P-X259P,X069S-X124I-X185Q-X218S, X069S-X128S-X166Q-X218S,X069S-X128S-X218S-X259P, X069S-X129P-X166Q-X185Q,X069S-X129P-X166Q-X218S, X069S-X129P-X166Q-X259P,X069S-X129P-X185Q-X218S, X069S-X166Q-X185Q-X218S,X069S-X166Q-X185Q-X259P, X069S-X166Q-X218S-X259P,X069S-X185Q-X218S-X259P, X076D-X078N-X124I-X218S,X076D-X078N-X128S-X259P, X076D-X078N-X129P-X185Q,X076D-X078N-X166Q-X185Q, X076D-X078N-X166Q-X218S,X076D-X078N-X166Q-X259P, X076D-X078N-X185Q-X218S,X076D-X078N-X185Q-X259P, X076D-X078N-X218S-X259P,X076D-X124I-X128S-X166Q, X076D-X124I-X128S-X259P,X076D-X128S-X166Q-X218S, X076D-X129P-X166Q-X259P,X076D-X129P-X185Q-X218S, X076D-X166Q-X185Q-X218S,X076D-X166Q-X185Q-X259P, X076D-X166Q-X218S-X259P,X076D-X185Q-X218S-X259P, X078N-X124I-X128S-X218S,X078N-X124I-X128S-X259P, X078N-X124I-X166Q-X259P,X078N-X128S-X166Q-X218S, X078N-X128S-X218S-X259P,X078N-X129P-X166Q-X259P, X078N-X129P-X185Q-X218S,X078N-X129P-X185Q-X259P, X078N-X166Q-X185Q-X218S,X078N-X166Q-X185Q-X259P, X078N-X166Q-X218S-X259P,X078N-X185Q-X218S-X259P, X124I-X128S-X166Q-X259P,X124I-X129P-X166Q-X259P, X124I-X166Q-X218S-X259P,X124I-X185Q-X218S-X259P, X128S-X129P-X166Q-X259P,X128S-X166Q-X185Q-X218S, X128S-X166Q-X185Q-X259P,X129P-X166Q-X185Q-X259P, X129P-X166Q-X218S-X259P,X129P-X185Q-X218S-X259P, and X166Q-X185Q-X218S-X259P, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides a subtilisin varianthaving at least two or more features selected from the group consistingof X003V-X009E, X003V-X040E, X003V-X069S, X003V-X076D, X003V-X078N,X003V-X166Q, X003V-X185Q, X003V-X218S, X003V-X259P, X009E-X040E,X009E-X069S, X009E-X076D, X009E-X078N, X009E-X166Q, X009E-X185Q,X009E-X218S, X009E-X259P, X040E-X069S, X040E-X076D, X040E-X078N,X040E-X166Q, X040E-X185Q, X040E-X218S, X040E-X259P, X069S-X076D,X069S-X078N, X069S-X166Q, X069S-X185Q, X069S-X218S, X069S-X259P,X076D-X078N, X076D-X166Q, X076D-X185Q, X076D-X218S, X076D-X259P,X078N-X166Q, X078N-X185Q, X078N-X218S, X078N-X259P, X166Q-X185Q,X166Q-X218S, X166Q-X259P, X185Q-X218S, X185Q-X259P, and X218S-X259P.

In yet another embodiment, the disclosure provides a subtilisin varianthaving at least three or more features selected from the groupconsisting of X003V-X009E-X040E, X003V-X009E-X069S, X003V-X009E-X076D,X003V-X009E-X078N, X003V-X009E-X166Q, X003V-X009E-X185Q,X003V-X009E-X218S, X003V-X009E-X259P, X003V-X040E-X069S,X003V-X040E-X076D, X003V-X040E-X078N, X003V-X040E-X166Q,X003V-X040E-X185Q, X003V-X040E-X218S, X003V-X040E-X259P,X003V-X069S-X076D, X003V-X069S-X078N, X003V-X069S-X166Q,X003V-X069S-X185Q, X003V-X069S-X218S, X003V-X069S-X259P,X003V-X076D-X078N, X003V-X076D-X166Q, X003V-X076D-X185Q,X003V-X076D-X218S, X003V-X076D-X259P, X003V-X078N-X166Q,X003V-X078N-X185Q, X003V-X078N-X218S, X003V-X078N-X259P,X003V-X166Q-X185Q, X003V-X166Q-X218S, X003V-X166Q-X259P,X003V-X185Q-X218S, X003V-X185Q-X259P, X003V-X218S-X259P,X009E-X040E-X069S, X009E-X040E-X076D, X009E-X040E-X078N,X009E-X040E-X166Q, X009E-X040E-X185Q, X009E-X040E-X218S,X009E-X040E-X259P, X009E-X069S-X076D, X009E-X069S-X078N,X009E-X069S-X166Q, X009E-X069S-X185Q, X009E-X069S-X218S,X009E-X069S-X259P, X009E-X076D-X078N, X009E-X076D-X166Q,X009E-X076D-X185Q, X009E-X076D-X218S, X009E-X076D-X259P,X009E-X078N-X166Q, X009E-X078N-X185Q, X009E-X078N-X218S,X009E-X078N-X259P, X009E-X166Q-X185Q, X009E-X166Q-X218S,X009E-X166Q-X259P, X009E-X185Q-X218S, X009E-X185Q-X259P,X009E-X218S-X259P, X040E-X069S-X076D, X040E-X069S-X078N,X040E-X069S-X166Q, X040E-X069S-X185Q, X040E-X069S-X218S,X040E-X069S-X259P, X040E-X076D-X078N, X040E-X076D-X166Q,X040E-X076D-X185Q, X040E-X076D-X218S, X040E-X076D-X259P,X040E-X078N-X166Q, X040E-X078N-X185Q, X040E-X078N-X218S,X040E-X078N-X259P, X040E-X166Q-X185Q, X040E-X166Q-X218S,X040E-X166Q-X259P, X040E-X185Q-X218S, X040E-X185Q-X259P,X040E-X218S-X259P, X069S-X076D-X078N, X069S-X076D-X166Q,X069S-X076D-X185Q, X069S-X076D-X218S, X069S-X076D-X259P,X069S-X078N-X166Q, X069S-X078N-X185Q, X069S-X078N-X218S,X069S-X078N-X259P, X069S-X166Q-X185Q, X069S-X166Q-X218S,X069S-X166Q-X259P, X069S-X185Q-X218S, X069S-X185Q-X259P,X069S-X218S-X259P, X076D-X078N-X166Q, X076D-X078N-X185Q,X076D-X078N-X218S, X076D-X078N-X259P, X076D-X166Q-X185Q,X076D-X166Q-X218S, X076D-X166Q-X259P, X076D-X185Q-X218S,X076D-X185Q-X259P, X076D-X218S-X259P, X078N-X166Q-X185Q,X078N-X166Q-X218S, X078N-X166Q-X259P, X078N-X185Q-X218S,X078N-X185Q-X259P, X078N-X218S-X259P, X166Q-X185Q-X218S,X166Q-X185Q-X259P, X166Q-X218S-X259P, and X185Q-X218S-X259P, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides subtilisin variantswith one or more mutations at E003, Q003, S003, T003, P009, S009, T009,A024, N024, S024, A040, P040, S040, A069, N076, D078, S078, T078, E079,L079, T079, V079, E087, N087, Q087, S087, G118, M118, N118, L124, M124,G128, I128, T128, A129, D129, S129, A130, M130, Q130, T130, V130, E145,Q145, S145, G166, S166, Q182, S182, N185, R185, S185, V185, L210, P210,F217, M217, Y217, N218, P218, T218, A248, N248, Q248, S248, D259, G259,and N259, where the positions are numbered by correspondence with theamino acid sequence of SEQ ID NO:1 (BPN′). In yet another embodiment,the disclosure provides variants of subtilisin AprE with one or moremutations at S003, S009, S024, P040, A069, N076, S078, S087, N118, M124,G128, T130, S145, G166, S182, P210, Y217, N218, and N259, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin AprE from the group consisting of 5003V, N076D, S078N, G166Q,Y217L, N218S, N259P, S009E, P040E, S003V-N259P, S003V-P040E,S003V-M124I, S003V-S078N, S003V-N076D, S003V-G166Q, S003V-G128S,A069S-N076D, A069S-N218S, A069S-G166Q, A069S-N259P, A069S-S078N,A069S-G128S, A069S-M124I, N076D-G128S, N076D-S078N, N076D-N218S,N076D-G166Q, N076D-M124I, S078T-M124I, S078N-G128S, S078N-N259P,S078N-N218S, S078N-G166Q, M124I-G166Q, M124I-N259P, M124I-G128S,M124I-N218S, G128S-N259P, G128S-N218S, G128S-G166Q, G166Q-N259P,G166Q-N218S, N218S-N259P, S003V-S009E, S003V-A069S, S003V-N218S,S009E-P040E, S009E-A069S, S009E-N076D, S009E-S078N, S009E-G166Q,S009E-N218S, S009E-N259P, P040E-A069S, P040E-N076D, P040E-S078N,P040E-G166Q, P040E-N218S, P040E-N259P, N076D-N259P, S003V-N076D-S078N,S003V-S078N-N218S, S003V-M124I-N259P, S003V-G128S-G166Q,S003V-G166Q-N218S, S003V-N218S-N259P, P040E-N076D-S078N,G128S-G166Q-N259P, S003V-S009E-P040E, S003V-S009E-A069S,S003V-S009E-N076D, S003V-S009E-S078N, S003V-S009E-G166Q,S003V-S009E-N218S, S003V-S009E-N259P, S003V-P040E-A069S,S003V-P040E-N076D, S003V-P040E-N218S, S003V-P040E-N259P,S003V-A069S-N076D, S003V-A069S-S078N, S003V-A069S-G166Q,S003V-A069S-N218S, S003V-A069S-N259P, S003V-N076D-G166Q,S003V-N076D-N218S, S003V-N076D-N259P, S003V-S078N-N259P,S003V-G166Q-N259P, S009E-P040E-A069S, S009E-P040E-N076D,S009E-P040E-S078N, S009E-P040E-G166Q, S009E-P040E-N218S,S009E-P040E-N259P, S009E-A069S-N076D, S009E-A069S-S078N,S009E-A069S-G166Q, S009E-A069S-N218S, S009E-A069S-N259P,S009E-N076D-S078N, S009E-N076D-G166Q, S009E-N076D-N218S,S009E-N076D-N259P, S009E-S078N-G166Q, S009E-S078N-N218S,S009E-S078N-N259P, S009E-G166Q-N218S, S009E-G166Q-N259P,S009E-N218S-N259P, P040E-A069S-S078N, P040E-A069S-G166Q,P040E-A069S-N218S, P040E-A069S-N259P, P040E-N076D-G166Q,P040E-N076D-N218S, P040E-N076D-N259P, P040E-S078N-G166Q,P040E-S078N-N218S, P040E-S078N-N259P, P040E-G166Q-N218S,P040E-G166Q-N259P, P040E-N218S-N259P, A069S-N076D-S078N,A069S-N076D-G166Q, A069S-N076D-N218S, A069S-N076D-N259P,A069S-S078N-G166Q, A069S-S078N-N218S, A069S-S078N-N259P,A069S-G166Q-N218S, A069S-G166Q-N259P, A069S-N218S-N259P,N076D-S078N-G166Q, N076D-S078N-N218S, N076D-S078N-N259P,N076D-G166Q-N218S, N076D-G166Q-N259P, N076D-N218S-N259P,S078N-G166Q-N218S, S078N-G166Q-N259P, S078N-N218S-N259P,G166Q-N218S-N259P, S003V-P040E-N076D-S078N, S003V-P040E-S078N-M124I,S003V-P040E-M124I-N218S, S003V-N076D-S078N-G128S,S003V-N076D-M124I-G166Q, S003V-N076D-G128S-N259P,S003V-N076D-G166Q-N259P, S003V-N076D-N218S-N259P,S003V-M124I-G128S-N218S, S003V-G128S-G166Q-N218S,P040E-N076D-S078N-G166Q, P040E-N076D-M124I-N218S,P040E-N076D-G166Q-N218S, P040E-N076D-G166Q-N259P,N076D-S078N-M124I-N218S, N076D-S078N-G128S-N259P,N076D-S078N-G166Q-N259P, N076D-M124I-G128S-G166Q,N076D-M124I-G128S-N259P, N076D-G128S-G166Q-N218S,S078N-G128S-G166Q-N218S, S078N-G128S-N218S-N259P,M124I-G166Q-N218S-N259P, S003V-P040E-A069S-G166Q,S003V-P040E-N076D-N218S, S003V-A069S-G166Q-N218S,S009E-P040E-A069S-N076D, S009E-P040E-A069S-N259P,S009E-P040E-S078N-N259P, S009E-P040E-G166Q-N218S,S009E-P040E-G166Q-N259P, S009E-P040E-N218S-N259P,S009E-A069S-S078N-G166Q, S009E-S078N-N218S-N259P,S009E-G166Q-N218S-N259P, P040E-A069S-N076D-S078N,P040E-A069S-S078N-G166Q, P040E-A069S-S078N-N259P,P040E-A069S-G166Q-N218S, N076D-S078N-G166Q-N218S, andN076D-G166Q-N218S-N259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′). Inyet another embodiment, the disclosure provides variants of subtilisinBad02409 with one or more mutations at T003, P009, S024, A069, N076,S078, V079, N087, G118, M124, G128, S129, M130, S145, G166, S182, N185,P210, Y217, N218, N248, and D259, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin Bad02409 from the group consisting of N076D, S078N, G128S,S182E, T003V-N218S, T003V-A069S, T003V-D259P, T003V-M124I, T003V-N076D,T003V-N185Q, T003V-G166Q, T003V-S078N, T003V-S129P, A069S-S129P,A069S-G166Q, A069S-N076D, A069S-S078N, N076D-S129P, S078N-N185Q,M124I-S129P, S129P-D259P, S129P-G166Q, G166Q-N218S, T003V-A069S-G166Q,T003V-N076D-D259P, T003V-S078N-N185Q, T003V-S129P-N185Q,T003V-G166Q-D259P, T003V-N185Q-D259P, A069S-N076D-G166Q,N076D-G166Q-N185Q, T003V-A069S-S078N-S129P, T003V-N076D-N185Q-D259P,T003V-S078N-S129P-N185Q, T003V-S078N-G166Q-D259P,T003V-G166Q-N185Q-D259P, A069S-N076D-S129P-D259P,A069S-S078N-S129P-N185Q, A069S-S129P-G166Q-N185Q,N076D-S078N-S129P-N185Q, N076D-S129P-G166Q-D259P, andN076D-G166Q-N185Q-D259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin Bba02069 with one or more mutations at Q003, T009, N024,P040, A069, N076, Q087, G118, M124, G128, S129, G166, S182, V185, P210,Y217, N218, Q248, and S259, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin Bba02069 from the group consisting of S129P, G118R, Q087D,N076D, M124I, Q248D, A069S, G128S, N024Q, Q003V, P040E, T009E, N218S,G166Q, S259P, Q003V-A069S, Q003V-V185Q, Q003V-S129P, Q003V-M124I,Q003V-G166Q, Q003V-G128S, Q003V-S259P, Q003V-N076D, P040E-V185Q,P040E-G166Q, A069S-G128S, A069S-S259P, A069S-M124I, A069S-G166Q,A069S-N076D, N076D-G128S, N076D-G166Q, N076D-M124I, N076D-S259P,N076D-S129P, M124I-G128S, M124I-V185Q, M124I-S129P, M124I-S259P,M124I-G166Q, M124I-N218S, G128S-S129P, G128S-G166Q, G128S-S259P,G128S-V185Q, S129P-G166Q, S129P-V185Q, S129P-S259P, G166Q-S259P,G166Q-V185Q, V185Q-S259P, V185Q-N218S, N218S-S259P, Q003V-T009E,Q003V-P040E, Q003V-N218S, T009E-P040E, T009E-A069S, T009E-N076D,T009E-G166Q, T009E-V185Q, T009E-N218S, T009E-S259P, P040E-A069S,P040E-N076D, P040E-N218S, P040E-S259P, A069S-V185Q, A069S-N218S,N076D-V185Q, N076D-N218S, G166Q-N218S, Q003V-P040E-G166Q,Q003V-G166Q-S259P, A069S-S129P-G166Q, A069S-S129P-V185Q,G128S-S129P-N218S, G128S-V185Q-N218S, Q003V-T009E-P040E,Q003V-T009E-A069S, Q003V-T009E-N076D, Q003V-T009E-G166Q,Q003V-T009E-V185Q, Q003V-T009E-N218S, Q003V-T009E-S259P,Q003V-P040E-A069S, Q003V-P040E-N076D, Q003V-P040E-V185Q,Q003V-P040E-N218S, Q003V-P040E-S259P, Q003V-A069S-N076D,Q003V-A069S-G166Q, Q003V-A069S-N218S, Q003V-A069S-S259P,Q003V-N076D-G166Q, Q003V-N076D-V185Q, Q003V-N076D-N218S,Q003V-N076D-S259P, Q003V-G166Q-V185Q, Q003V-G166Q-N218S,Q003V-V185Q-S259P, Q003V-N218S-S259P, T009E-P040E-A069S,T009E-P040E-N076D, T009E-P040E-G166Q, T009E-P040E-V185Q,T009E-P040E-N218S, T009E-P040E-S259P, T009E-A069S-N076D,T009E-A069S-G166Q, T009E-A069S-V185Q, T009E-A069S-N218S,T009E-A069S-S259P, T009E-N076D-G166Q, T009E-N076D-V185Q,T009E-N076D-N218S, T009E-N076D-S259P, T009E-G166Q-V185Q,T009E-G166Q-N218S, T009E-G166Q-S259P, T009E-V185Q-N218S,T009E-V185Q-S259P, T009E-N218S-S259P, P040E-A069S-N076D,P040E-A069S-G166Q, P040E-A069S-V185Q, P040E-A069S-N218S,P040E-A069S-S259P, P040E-N076D-G166Q, P040E-N076D-V185Q,P040E-N076D-N218S, P040E-N076D-S259P, P040E-G166Q-V185Q,P040E-G166Q-N218S, P040E-G166Q-S259P, P040E-V185Q-N218S,P040E-V185Q-S259P, P040E-N218S-S259P, A069S-N076D-G166Q,A069S-N076D-V185Q, A069S-N076D-N218S, A069S-N076D-S259P,A069S-G166Q-V185Q, A069S-G166Q-N218S, A069S-G166Q-S259P,A069S-V185Q-N218S, A069S-V185Q-S259P, A069S-N218S-S259P,N076D-G166Q-V185Q, N076D-G166Q-N218S, N076D-G166Q-S259P,N076D-V185Q-N218S, N076D-V185Q-S259P, N076D-N218S-S259P,G166Q-V185Q-N218S, G166Q-V185Q-S259P, G166Q-N218S-S259P,V185Q-N218S-S259P, Q003V-A069S-S129P-S259P, Q003V-M124I-G128S-G166Q,Q003V-G128S-S129P-V185Q, P040E-A069S-S129P-N218S,P040E-M124I-N218S-S259P, A069S-N076D-S129P-G166Q,A069S-M124I-S129P-S259P, A069S-M124I-V185Q-N218S,G128S-G166Q-V185Q-N218S, S129P-G166Q-V185Q-S259P,Q003V-T009E-P040E-G166Q, Q003V-T009E-P040E-V185Q,Q003V-T009E-N076D-N218S, Q003V-T009E-G166Q-V185Q,Q003V-P040E-N076D-V185Q, T009E-P040E-A069S-V185Q,T009E-P040E-A069S-N218S, T009E-P040E-N076D-V185Q,T009E-A069S-N076D-N218S, T009E-A069S-G166Q-V185Q,T009E-A069S-G166Q-N218S, T009E-A069S-V185Q-N218S,T009E-N076D-V185Q-S259P, T009E-V185Q-N218S-S259P,P040E-A069S-N076D-V185Q, P040E-A069S-G166Q-N218S,P040E-A069S-V185Q-N218S, P040E-A069S-V185Q-S259P,P040E-A069S-N218S-S259P, P040E-N076D-G166Q-V185Q,P040E-N076D-V185Q-N218S, P040E-N076D-V185Q-S259P,P040E-G166Q-V185Q-N218S, P040E-V185Q-N218S-S259P,A069S-N076D-G166Q-V185Q, A069S-N076D-G166Q-N218S,A069S-N076D-G166Q-S259P, A069S-N076D-V185Q-N218S,A069S-N076D-N218S-S259P, A069S-G166Q-V185Q-N218S,N076D-G166Q-V185Q-S259P, N076D-G166Q-N218S-S259P, andG166Q-V185Q-N218S-S259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin Bpan01744 with one or more mutations at 5003, S009, S024,A069, N076, S078, N087, G118, M124, T128, S129, A130, G166, Q182, N185,P210, N218, N248, and N259, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin Bpan01744 from the group consisting of 5003V, S078N, S009E,N076D, N185Q, N218S, N259P, S003V-N185Q, S003V-N076D, S003V-A069S,S003V-S078N, S003V-N218S, S003V-N259P, A069S-N076D, A069S-G166Q,A069S-N185Q, A069S-S078N, A069S-N218S, N076D-S078N, N076D-S129P,S078N-G166Q, S078N-M124I, S078N-S129P, M124I-N218S, M124I-S129P,M124I-N185Q, S129P-N259P, S129P-N185Q, S129P-N218S, S129P-G166Q,G166Q-N259P, G166Q-N218S, G166Q-N185Q, N185Q-N218S, N185Q-N259P,N218S-N259P, S003V-S009E, S003V-G166Q, S009E-N076D, S009E-S078N,S009E-G166Q, S009E-N185Q, S009E-N218S, S009E-N259P, N076D-G166Q,N076D-N185Q, N076D-N218S, N076D-N259P, S078N-N185Q, S078N-N218S,S078N-N259P, S003V-A069S-N076D, S003V-A069S-S129P, S003V-A069S-N185Q,S003V-N076D-S129P, S003V-N076D-N185Q, S003V-S078N-G166Q,S003V-S129P-N259P, S003V-G166Q-N218S, A069S-N076D-N185Q,A069S-G166Q-N185Q, N076D-S078N-G166Q, N076D-S129P-N218S,S078N-S129P-N259P, S078N-N185Q-N259P, S003V-S009E-A069S,S003V-S009E-N076D, S003V-S009E-S078N, S003V-S009E-N185Q,S003V-S009E-N218S, S003V-S009E-N259P, S003V-A069S-S078N,S003V-A069S-N218S, S003V-N076D-S078N, S003V-N076D-G166Q,S003V-N076D-N218S, S003V-S078N-N185Q, S003V-S078N-N218S,S003V-S078N-N259P, S003V-N185Q-N218S, S003V-N185Q-N259P,S003V-N218S-N259P, S009E-A069S-N076D, S009E-A069S-S078N,S009E-A069S-G166Q, S009E-A069S-N259P, S009E-N076D-S078N,S009E-N076D-G166Q, S009E-N076D-N185Q, S009E-N076D-N218S,S009E-N076D-N259P, S009E-S078N-N185Q, S009E-S078N-N218S,S009E-S078N-N259P, S009E-G166Q-N185Q, S009E-G166Q-N218S,S009E-N185Q-N218S, S009E-N185Q-N259P, S009E-N218S-N259P,A069S-N076D-S078N, A069S-N076D-G166Q, A069S-N076D-N218S,A069S-N076D-N259P, A069S-S078N-N185Q, A069S-S078N-N218S,A069S-S078N-N259P, A069S-G166Q-N218S, A069S-N185Q-N218S,A069S-N218S-N259P, N076D-S078N-N185Q, N076D-S078N-N218S,N076D-S078N-N259P, N076D-G166Q-N218S, N076D-N185Q-N218S,N076D-N185Q-N259P, S078N-G166Q-N218S, S078N-N185Q-N218S,S078N-N218S-N259P, G166Q-N185Q-N218S, N185Q-N218S-N259P,S003V-A069S-N076D-S078N, S003V-A069S-N076D-N185Q,S003V-A069S-N076D-N259P, S003V-A069S-S078N-S129P,S003V-A069S-S078N-N185Q, S003V-A069S-S129P-N218S,S003V-A069S-N185Q-N259P, S003V-N076D-S129P-G166Q,S003V-N076D-S129P-N185Q, S003V-N076D-S129P-N259P,S003V-S078N-N185Q-N218S, S003V-S078N-N185Q-N259P,S003V-G166Q-N185Q-N259P, S003V-N185Q-N218S-N259P,A069S-N076D-S078N-N218S, A069S-N076D-N185Q-N259P,A069S-S078N-N185Q-N218S, A069S-S129P-G166Q-N218S,A069S-S129P-N185Q-N218S, A069S-G166Q-N218S-N259P,A069S-N185Q-N218S-N259P, N076D-S078N-S129P-N185Q,N076D-S078N-N185Q-N218S, N076D-S129P-N185Q-N218S,N076D-G166Q-N185Q-N259P, S078N-S129P-G166Q-N259P,S078N-S129P-N185Q-N259P, S078N-G166Q-N218S-N259P,S129P-G166Q-N218S-N259P, S129P-N185Q-N218S-N259P,S003V-S009E-A069S-N185Q, S003V-S009E-N218S-N259P,S003V-A069S-N076D-N218S, S003V-A069S-N185Q-N218S,S003V-A069S-N218S-N259P, S003V-N076D-N218S-N259P,S003V-G166Q-N185Q-N218S, S009E-A069S-N076D-S078N,S009E-A069S-S078N-G166Q, S009E-A069S-S078N-N218S,S009E-A069S-G166Q-N218S, S009E-A069S-N218S-N259P,S009E-N076D-S078N-G166Q, S009E-N076D-S078N-N185Q,S009E-N076D-N218S-N259P, S009E-S078N-N185Q-N218S,S009E-S078N-N218S-N259P, S009E-G166Q-N185Q-N218S,A069S-N076D-S078N-N259P, A069S-S078N-G166Q-N218S,A069S-S078N-N185Q-N259P, A069S-S078N-N218S-N259P,N076D-S078N-G166Q-N185Q, N076D-S078N-G166Q-N218S,N076D-S078N-N218S-N259P, N076D-G166Q-N185Q-N218S,N076D-G166Q-N218S-N259P, N076D-N185Q-N218S-N259P,S078N-G166Q-N185Q-N218S, and S078N-G166Q-N185Q-N259P, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspAI02518 with one or more mutations at T003, S009, A069,N076, S078, S087, G118, M124, G128, T130, S166, S182, N185, P210, N218,Q248, and N259, where the positions are numbered by correspondence withthe amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspAI02518 from the group consisting of S003V, S009E, N076D,S078N, M124I, S182E, N185Q, N218S, N259P, S166Q, S003V-N259P,S003V-N218S, S003V-A069S, S003V-N185Q, S003V-G128S, S003V-M124I,S003V-N076D, S003V-S166Q, A069S-N218S, A069S-N076D, A069S-S078N,A069S-N185Q, A069S-S166Q, N076D-N218S, N076D-N259P, N076D-G128S,N076D-M124I, N076D-N185Q, N076D-S078N, S078N-M124I, S078N-N218S,S078N-N259P, S078N-G128S, S078N-N185Q, M124I-G128S, M124I-S166Q,M124I-N185Q, S166Q-N218S, S166Q-N259P, N185Q-N259P, N218S-N259P,S003V-S009E, S003V-S078N, S009E-A069S, S009E-N076D, S009E-S078N,S009E-S166Q, S009E-N185Q, S009E-N218S, S009E-N259P, A069S-N259P,N076D-S166Q, S078N-S166Q, S166Q-N185Q, N185Q-N218S, S003V-A069S-N185Q,S003V-S078N-G128S, S003V-N185Q-N259P, A069S-N076D-G128S,A069S-N076D-N218S, A069S-S078N-M124I, N076D-S078N-N185Q,N076D-S078N-N218S, N076D-G128S-S166Q, M124I-G128S-N185Q,G128S-S166Q-N185Q, S003V-S009E-A069S, S003V-S009E-N076D,S003V-S009E-S078N, S003V-S009E-S166Q, S003V-S009E-N185Q,S003V-S009E-N218S, S003V-S009E-N259P, S003V-A069S-N076D,S003V-A069S-S078N, S003V-A069S-N218S, S003V-N076D-S078N,S003V-N076D-S166Q, S003V-N076D-N185Q, S003V-N076D-N218S,S003V-N076D-N259P, S003V-S078N-S166Q, S003V-S078N-N185Q,S003V-S078N-N218S, S003V-S078N-N259P, S003V-S166Q-N185Q,S003V-S166Q-N259P, S003V-N185Q-N218S, S003V-N218S-N259P,S009E-A069S-N076D, S009E-A069S-N185Q, S009E-A069S-N218S,S009E-N076D-S078N, S009E-N076D-S166Q, S009E-N076D-N185Q,S009E-N076D-N218S, S009E-N076D-N259P, S009E-S078N-S166Q,S009E-S078N-N185Q, S009E-S078N-N218S, S009E-S078N-N259P,S009E-S166Q-N185Q, S009E-S166Q-N218S, S009E-S166Q-N259P,S009E-N185Q-N218S, S009E-N185Q-N259P, S009E-N218S-N259P,A069S-N076D-S078N, A069S-N076D-S166Q, A069S-N076D-N185Q,A069S-N076D-N259P, A069S-S078N-S166Q, A069S-S078N-N218S,A069S-S166Q-N185Q, A069S-S166Q-N218S, A069S-S166Q-N259P,A069S-N185Q-N218S, A069S-N218S-N259P, N076D-S078N-5166Q,N076D-S078N-N259P, N076D-5166Q-N185Q, N076D-5166Q-N218S,N076D-5166Q-N259P, N076D-N185Q-N218S, N076D-N185Q-N259P,N076D-N218S-N259P, S078N-S166Q-N185Q, S078N-S166Q-N218S,S078N-S166Q-N259P, S078N-N185Q-N218S, S078N-N185Q-N259P,S078N-N218S-N259P, S166Q-N185Q-N218S, S166Q-N185Q-N259P,S166Q-N218S-N259P, S003V-A069S-N076D-G128S, S003V-A069S-S078N-G128S,S003V-A069S-S078N-S166Q, S003V-A069S-M124I-N218S,S003V-A069S-G128S-S166Q, S003V-A069S-G128S-N259P,S003V-N076D-S166Q-N185Q, S003V-S078N-M124I-S166Q,S003V-S078N-G128S-N185Q, S003V-S078N-G128S-N218S,S003V-M124I-S166Q-N259P, S003V-M124I-N185Q-N259P,S003V-G128S-N185Q-N218S, S003V-G128S-N218S-N259P,S003V-S166Q-N218S-N259P, A069S-N076D-S078N-G128S,A069S-N076D-M124I-G128S, A069S-N076D-S166Q-N218S,A069S-N076D-N185Q-N259P, A069S-N076D-N218S-N259P,A069S-S078N-G128S-N218S, A069S-S078N-N185Q-N259P,A069S-M124I-G128S-N185Q, A069S-M124I-G128S-N218S,A069S-G128S-S166Q-N218S, A069S-G128S-N218S-N259P,N076D-S166Q-N185Q-N259P, S078N-M124I-G128S-N218S,S078N-N185Q-N218S-N259P, M124I-G128S-S166Q-N259P,M124I-S166Q-N218S-N259P, G128S-S166Q-N185Q-N259P,S003V-S009E-N076D-S166Q, S003V-A069S-S078N-N259P,S003V-A069S-S166Q-N218S, S003V-N076D-S078N-S166Q,S003V-N076D-S078N-N259P, S003V-N076D-S166Q-N259P,S003V-S166Q-N185Q-N259P, S009E-A069S-N076D-S166Q,S009E-A069S-N076D-N218S, S009E-A069S-N076D-N259P,S009E-A069S-S078N-S166Q, S009E-A069S-S078N-N218S,S009E-A069S-S166Q-N259P, S009E-N076D-S078N-N259P,S009E-N076D-S166Q-N185Q, S009E-N076D-S166Q-N259P,S009E-N076D-N185Q-N218S, S009E-N076D-N185Q-N259P,S009E-S078N-S166Q-N218S, S009E-S078N-N185Q-N259P,S009E-S078N-N218S-N259P, A069S-N076D-S078N-N218S,A069S-N076D-S166Q-N185Q, A069S-N076D-N185Q-N218S,A069S-S078N-S166Q-N218S, A069S-S078N-N185Q-N218S,A069S-S078N-N218S-N259P, A069S-S166Q-N185Q-N218S,A069S-S166Q-N185Q-N259P, N076D-S078N-S166Q-N218S,N076D-S078N-N185Q-N218S, N076D-S078N-N185Q-N259P,N076D-S078N-N218S-N259P, N076D-S166Q-N185Q-N218S,N076D-S166Q-N218S-N259P, N076D-N185Q-N218S-N259P,S078N-S166Q-N185Q-N218S, S078N-S166Q-N185Q-N259P, andS166Q-N185Q-N218S-N259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspAK01305 with one or more mutations at S003, S024, S040,A069, D078, E079, E087, N118, L124, S145, G166, Q182, S185, P210, S248,and D259, where the positions are numbered by correspondence with theamino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspAK01305 from the group consisting of S003V, S040E, G166Q,S185Q, P210I, S003V-S185Q, S003V-G166Q, S003V-R262L, S003V-S040E,S040E-G166Q, S040E-S185Q, and G166Q-S185Q, where the positions arenumbered by correspondence with the amino acid sequence of SEQ ID NO:1(BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspZ00056 with one or more mutations at T003, P009, A024,A069, D078, L079, Q087, G118, M124, G128, S129, Q130, E145, G166, Q182,N185, P210, F217, N218, N248, and G259, where the positions are numberedby correspondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspZ00056 from the group consisting of Q182E, G128S, E145R,M124I, N218S, S129P, T003V, P009E, A069S, G166Q, N185Q, G259P,G128S-S129P, G128S-N218S, A069S-N185Q, A069S-D078N, D078N-G166Q,G166Q-N185Q, T003V-M124I, G128S-N185Q, A069S-G128S, M124I-N185Q,G166Q-G259P, A069S-G259P, S129P-G166Q, T003V-G259P, T003V-N185Q,D078N-G259P, M124I-N218S, G128S-G166Q, A069S-M124I, S129P-N185Q,G128S-G259P, T003V-G166Q, T003V-G128S, T003V-A069S, M124I-G166Q,M124I-S129P, N218S-G259P, N185Q-G259P, D078N-S129P, M124I-G128S,T003V-N218S, A069S-G166Q, P009E-G166Q, P009E-G259P, A069S-N218S,G166Q-N218S, N185Q-N218S, T003V-S129P-G166Q, T003V-S129P-N185Q,T003V-S129P-G259P, T003V-N185Q-N218S, A069S-G128S-N185Q,A069S-S129P-G259P, A069S-G166Q-N185Q, A069S-G166Q-N218S,M124I-S129P-N185Q, M124I-S129P-G259P, M124I-N185Q-G259P,M124I-N218S-G259P, G128S-G166Q-G259P, G128S-N185Q-G259P,G166Q-N218S-G259P, T003V-P009E-G166Q, T003V-A069S-G166Q,T003V-A069S-G259P, T003V-G166Q-N185Q, T003V-G166Q-N218S,T003V-G166Q-G259P, T003V-N185Q-G259P, T003V-N218S-G259P,P009E-A069S-G166Q, P009E-A069S-G259P, P009E-G166Q-N185Q,P009E-G166Q-N218S, P009E-G166Q-G259P, P009E-N218S-G259P,A069S-G166Q-G259P, A069S-N185Q-G259P, A069S-N218S-G259P,G166Q-N185Q-G259P, N185Q-N218S-G259P, T003V-A069S-G128S-N185Q,T003V-A069S-N185Q-G259P, T003V-A069S-N218S-G259P,T003V-M124I-G166Q-G259P, T003V-N185Q-N218S-G259P,A069S-S129P-G166Q-G259P, M124I-S129P-G166Q-G259P,M124I-G166Q-N218S-G259P, M124I-N185Q-N218S-G259P,G128S-S129P-G166Q-G259P, S129P-G166Q-N185Q-G259P,T003V-P009E-A069S-G166Q, T003V-P009E-G166Q-G259P,T003V-A069S-G166Q-N185Q, T003V-G166Q-N218S-G259P,P009E-A069S-G166Q-N218S, P009E-G166Q-N185Q-N218S,P009E-G166Q-N185Q-G259P, P009E-G166Q-N218S-G259P,P009E-N185Q-N218S-G259P, A069S-G166Q-N185Q-N218S,A069S-G166Q-N185Q-G259P, A069S-G166Q-N218S-G259P, andG166Q-N185Q-N218S-G259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspZ00258 with one or more mutations at E003, N024, A069,D078, L079, N118, M124, G128, A129, V130, Q145, G166, S182, N185, L210,N218, A248, and D259, where the positions are numbered by correspondencewith the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin BspZ00258 from the group consisting of E003V, G166Q, D259P,A069S-N185Q, A069S-N218S, A129P-D259P, G166Q-N185Q, G166Q-D259P,E003V-A069S-G128S, E003V-G128S-D259P, E003V-A129P-N185Q,A069S-A129P-G166Q, E003V-A069S-G128S-N185Q, E003V-A069S-A129P-N185Q,E003V-G128S-N185Q-D259P, and E003V-A129P-N185Q-N218S, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin Chemgen_164A with one or more mutations at T003, T009, S024,P040, A069, N076, T078, N087, N118, M124, G128, S129, 5145, G166, S182,N185, P210, Y217, N218, and D259, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin Chemgen_164A from the group consisting of T003V, A069S,N087D, N118R, S129P, G166Q, S182E, N218S, P040E, N076D, T078N, N185Q,T003V-N076D, T003V-N185Q, T003V-G128S, T003V-S129P, T003V-G166Q,T003V-T078N, T003V-A069S, T003V-M124I, T003V-N218S, P040E-M124I,A069S-G128S, A069S-G166Q, A069S-T078N, A069S-D259P, A069S-S129P,A069S-N076D, A069S-N218S, A069S-N185Q, N076D-G166Q, N076D-N218S,N076D-M124I, N076D-T078N, N076D-D259P, N076D-S129P, N076D-G128S,T078N-G128S, T078N-N185Q, T078N-N218S, T078N-D259P, T078N-S129P,T078N-M124I, T078N-G166Q, G128S-N218S, G128S-D259P, G128S-N185Q,S129P-N185Q, S129P-G166Q, S129P-N218S, G166Q-D259P, G166Q-N185Q,G166Q-N218S, N185Q-N218S, N185Q-D259P, N218S-D259P, T003V-T009E,T003V-P040E, T003V-D259P, T009E-A069S, T009E-N076D, T009E-T078N,T009E-G166Q, T009E-N185Q, T009E-D259P, P040E-T078N, P040E-G166Q,P040E-N185Q, P040E-N218S, N076D-N185Q, T003V-T009E-P040E,T003V-T009E-A069S, T003V-T009E-N185Q, T003V-P040E-N076D,T003V-P040E-G166Q, T003V-P040E-N185Q, T003V-P040E-D259P,T003V-A069S-N076D, T003V-A069S-T078N, T003V-A069S-G166Q,T003V-A069S-N185Q, T003V-A069S-N218S, T003V-A069S-D259P,T003V-N076D-T078N, T003V-N076D-G166Q, T003V-N076D-N185Q,T003V-N076D-N218S, T003V-N076D-D259P, T003V-T078N-G166Q,T003V-T078N-N185Q, T003V-T078N-D259P, T003V-G166Q-N185Q,T003V-G166Q-D259P, T003V-N185Q-N218S, T003V-N185Q-D259P,T003V-N218S-D259P, T009E-P040E-A069S, T009E-P040E-N076D,T009E-P040E-T078N, T009E-P040E-G166Q, T009E-P040E-N218S,T009E-P040E-D259P, T009E-A069S-N076D, T009E-A069S-T078N,T009E-A069S-G166Q, T009E-A069S-N218S, T009E-A069S-D259P,T009E-N076D-T078N, T009E-N076D-G166Q, T009E-N076D-N185Q,T009E-N076D-N218S, T009E-N076D-D259P, T009E-T078N-G166Q,T009E-T078N-N185Q, T009E-T078N-N218S, T009E-T078N-D259P,T009E-G166Q-N218S, T009E-G166Q-D259P, T009E-N185Q-N218S,T009E-N185Q-D259P, P040E-A069S-N076D, P040E-A069S-T078N,P040E-A069S-G166Q, P040E-A069S-D259P, P040E-N076D-T078N,P040E-N076D-G166Q, P040E-N076D-N185Q, P040E-N076D-N218S,P040E-T078N-N185Q, P040E-T078N-D259P, P040E-G166Q-N185Q,P040E-G166Q-N218S, P040E-G166Q-D259P, P040E-N185Q-N218S,P040E-N185Q-D259P, P040E-N218S-D259P, A069S-N076D-T078N,A069S-N076D-G166Q, A069S-N076D-N185Q, A069S-N076D-N218S,A069S-N076D-D259P, A069S-T078N-G166Q, A069S-T078N-N185Q,A069S-T078N-N218S, A069S-T078N-D259P, A069S-G166Q-N218S,A069S-G166Q-D259P, A069S-N185Q-N218S, A069S-N185Q-D259P,A069S-N218S-D259P, N076D-T078N-G166Q, N076D-T078N-N218S,N076D-T078N-D259P, N076D-G166Q-N218S, N076D-G166Q-D259P,N076D-N185Q-N218S, N076D-N218S-D259P, T078N-G166Q-N185Q,T078N-G166Q-N218S, T078N-N185Q-D259P, T078N-N218S-D259P,G166Q-N185Q-N218S, G166Q-N185Q-D259P, G166Q-N218S-D259P,N185Q-N218S-D259P, T003V-T009E-P040E-N185Q, T003V-T009E-A069S-T078N,T003V-P040E-G166Q-D259P, T003V-N076D-T078N-D259P,T003V-N185Q-N218S-D259P, T009E-P040E-A069S-T078N,T009E-P040E-A069S-N185Q, T009E-P040E-A069S-D259P,T009E-P040E-N076D-T078N, T009E-P040E-T078N-N185Q,T009E-P040E-N185Q-N218S, T009E-P040E-N185Q-D259P,T009E-A069S-N076D-G166Q, T009E-A069S-N076D-N185Q,T009E-N076D-G166Q-N218S, T009E-T078N-G166Q-N185Q,P040E-A069S-T078N-N218S, P040E-A069S-G166Q-N218S,P040E-A069S-G166Q-D259P, P040E-N076D-T078N-N185Q,P040E-N076D-T078N-N218S, P040E-N076D-G166Q-D259P,P040E-T078N-N185Q-D259P, P040E-T078N-N218S-D259P,A069S-N076D-T078N-N185Q, A069S-N076D-T078N-D259P,A069S-N076D-G166Q-D259P, A069S-T078N-G166Q-N185Q,A069S-T078N-N185Q-D259P, N076D-T078N-G166Q-N218S,N076D-T078N-G166Q-D259P, N076D-T078N-N218S-D259P, andT078N-N185Q-N218S-D259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin CP474 with one or more mutations at T003, P009, S024, A040,A069, T078, T079, 5087, G118, L124, 5166, Q182, N185, P210, N218, N248,and D259, where the positions are numbered by correspondence with theamino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin CP474 from the group consisting of T003V, A040E, A069S,T078N, T079I, S166Q, N185Q, T003V-5166Q, T003V-N185Q, T003V-N218S,T003V-A040E, T003V-D259P, T003V-A069S, T003V-T078N, T003V-T079I,T003V-L124I, A040E-S166Q, A040E-N185Q, A040E-N218S, A040E-D259P,A040E-A069S, A040E-T078N, A040E-T079I, A040E-L124I, A069S-N185Q,A069S-T078N, A069S-T079I, A069S-S166Q, T078N-D259P, T078N-T079I,T078N-S166Q, T078N-N185Q, T078N-N218S, T079I-L124I, T079I-S166Q,T079I-N185Q, T079I-N218S, T079I-D259P, S166Q-N218S, N185Q-D259P,N185Q-N218S, and N218S-D259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin DSM14391 with one or more mutations at T003, T009, S024,S040, A069, N076, S078, S087, N118, M124, D129, A130, G166, Q182, R185,L210, M217, P218, N248, and N259, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin DSM14391 from the group consisting of T003V, T009E, S024Q,S040E, A069S, N076D, S078N, A130S, G166Q, Q182E, R185Q, P218S, N248D,N259P, T003V-R185Q, T003V-A069S, T003V-G166Q, T003V-N259P, T003V-N076D,T003V-S078N, T003V-P218S, S040E-S078N, A069S-S078N, A069S-N259P,A069S-R185Q, A069S-P218S, A069S-N076D, N076D-S078N, N076D-P218S,N076D-D129P, S078N-D129P, S078N-N259P, S078N-M124I, S078N-P218S,S078N-R185Q, M124I-G166Q, M124I-P218S, M124I-N259K, D129P-P218S,D129P-G166Q, D129P-R185Q, D129P-N259P, G166Q-R185Q, G166Q-N259P,R185Q-P218S, R185Q-N259P, T003V-T009E, T003V-S040E, T009E-S040E,T009E-A069S, T009E-N076D, T009E-S078N, T009E-R185Q, T009E-P218S,T009E-N259P, S040E-A069S, S040E-N076D, S040E-R185Q, S040E-P218S,S040E-N259P, N076D-R185Q, N076D-N259P, G166Q-P218S, P218S-N259P,T003V-S040E-P218S, T003V-G166Q-P218S, T003V-G166Q-N259P,S040E-N076D-G166Q, S040E-N076D-R185Q, S040E-S078N-D129P,S040E-R185Q-P218S, S040E-R185Q-N259P, A069S-S078N-N259P,A069S-D129P-P218S, A069S-P218S-N259P, N076D-R185Q-P218S,N076D-P218S-N259P, S078N-R185Q-P218S, S078N-P218S-N259P,T003V-T009E-S040E, T003V-T009E-A069S, T003V-T009E-N076D,T003V-T009E-S078N, T003V-T009E-R185Q, T003V-T009E-P218S,T003V-T009E-N259P, T003V-S040E-A069S, T003V-S040E-N076D,T003V-S040E-S078N, T003V-S040E-R185Q, T003V-S040E-N259P,T003V-A069S-N076D, T003V-A069S-R185Q, T003V-A069S-P218S,T003V-N076D-S078N, T003V-N076D-R185Q, T003V-N076D-P218S,T003V-N076D-N259P, T003V-S078N-R185Q, T003V-S078N-P218S,T003V-S078N-N259P, T003V-R185Q-P218S, T003V-R185Q-N259P,T003V-P218S-N259P, T009E-S040E-N076D, T009E-S040E-S078N,T009E-S040E-R185Q, T009E-S040E-P218S, T009E-S040E-N259P,T009E-A069S-S078N, T009E-A069S-P218S, T009E-A069S-N259P,T009E-N076D-S078N, T009E-N076D-R185Q, T009E-N076D-P218S,T009E-N076D-N259P, T009E-S078N-R185Q, T009E-S078N-P218S,T009E-S078N-N259P, T009E-G166Q-P218S, T009E-R185Q-P218S,T009E-R185Q-N259P, T009E-P218S-N259P, S040E-A069S-N076D,S040E-A069S-R185Q, S040E-A069S-P218S, S040E-A069S-N259P,S040E-N076D-S078N, S040E-N076D-P218S, S040E-N076D-N259P,S040E-S078N-R185Q, S040E-S078N-P218S, S040E-S078N-N259P,S040E-G166Q-P218S, S040E-P218S-N259P, A069S-N076D-S078N,A069S-N076D-R185Q, A069S-N076D-P218S, A069S-N076D-N259P,A069S-S078N-R185Q, A069S-S078N-P218S, A069S-G166Q-P218S,A069S-R185Q-P218S, A069S-R185Q-N259P, N076D-S078N-R185Q,N076D-S078N-P218S, N076D-S078N-N259P, N076D-G166Q-P218S,S078N-G166Q-P218S, S078N-R185Q-N259P, G166Q-R185Q-P218S,G166Q-P218S-N259P, R185Q-P218S-N259P, T003V-S040E-A069S-N076D,T003V-S040E-N076D-S078N, T003V-S040E-N076D-D129P,T003V-S040E-G166Q-R185Q, T003V-S040E-G166Q-N259P,T003V-A069S-R185Q-N259P, T003V-N076D-S078N-N259P,T003V-N076D-R185Q-N259P, T003V-S078N-D129P-N259P,T003V-S078N-P218S-N259P, S040E-N076D-S078N-R185Q,S040E-N076D-P218S-N259P, S040E-S078N-G166Q-P218S,S040E-R185Q-P218S-N259P, A069S-D129P-R185Q-P218S,A069S-R185Q-P218S-N259P, S078N-D129P-R185Q-P218S,D129P-R185Q-P218S-N259P, T003V-T009E-S040E-N076D,T003V-A069S-S078N-P218S, T003V-G166Q-R185Q-P218S,T003V-R185Q-P218S-N259P, T009E-S040E-A069S-P218S,T009E-A069S-N076D-R185Q, T009E-N076D-S078N-R185Q,T009E-N076D-G166Q-P218S, T009E-S078N-R185Q-P218S,S040E-A069S-S078N-P218S, S040E-A069S-G166Q-P218S,S040E-N076D-G166Q-R185Q, S040E-N076D-G166Q-P218S,A069S-N076D-S078N-N259P, A069S-S078N-R185Q-P218S,N076D-S078N-G166Q-R185Q, S078N-G166Q-P218S-N259P, andS078N-R185Q-P218S-N259P, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin WP_082194748 with one or more mutations at T003, P009, A024,P040, A069, T078, S087, N118, M124, G128, G166, S182, V185, P210, Y217,T218, Q248, and S259, where the positions are numbered by correspondencewith the amino acid sequence of SEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin WP_082194748 from the group consisting of Y217L, S087D,T078N, G128S, G166Q, S182E, G128S-V185Q, A069S-G128S, T078N-V185Q,V185Q-S259P, G166Q-V185Q, T078N-S259P, T003V-G128S, T078N-G128S,G128S-S259P, G166Q-S259P, A069S-M124I, T003V-M124I, M124I-S259P,M124I-V185Q, T003V-S259P, A069S-S259P, M124I-G128S, A069S-G166Q,T078N-M124I, M124I-G166Q, T078N-G166Q, T003V-G166Q, T003V-T078N-G166Q,T003V-T078N-S259P, T003V-M124I-G128S, T003V-G128S-G166Q,T003V-G128S-S259P, T003V-G166Q-S259P, T078N-M124I-G166Q,T078N-G128S-G166Q, T078N-G166Q-S259P, M124I-G128S-G166Q,M124I-G166Q-S259P, T003V-T078N-M124I-G166Q, T003V-T078N-G166Q-S259P,T003V-M124I-G128S-S259P, T003V-M124I-G166Q-S259P,T078N-M124I-G128S-S259P, and T078N-M124I-G166Q-S259P, where thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin ZP-00454 with one or more mutations at P009, S024, A040,A069, N076, T078, T079, N087, M118, M124, I128, S129, T130, S145, G166,S182, N185, P210, F217, N218, N248, and D259, where the positions arenumbered by correspondence with the amino acid sequence of SEQ ID NO:1(BPN′).

In yet another embodiment, the disclosure provides variants ofsubtilisin ZP-00454 from the group consisting of A040E, A069S, N076D,T078N, T079I, I128S, A040E-M124I, A040E-I128S, A040E-S129P, A040E-G166Q,A040E-A069S, A040E-N185Q, A040E-N076D, A040E-N218S, A040E-T078N,A040E-D259P, A069S-N076D, A069S-N218S, A069S-T078N, A069S-T079I,A069S-1128S, A069S-S129P, A069S-N185Q, N076D-N185Q, N076D-N218S,N076D-T078N, N076D-D259P, N076D-T079I, N076D-M124I, N076D-I128S,N076D-S129P, N076D-G166Q, T078N-N185Q, T078N-D259P, T078N-T079I,T078N-I128S, T078N-S129P, T078N-G166Q, T079I-N218S, T079I-D259P,T079I-M124I, T07914128S, T079I-S129P, T079I-G166Q, T079I-N185Q,1128S-S129P, and S129P-G166Q, where the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′).

The subtilisin variants having at least one, two, three, four, or morefeatures selected from the group consisting of: X003T, X003V, X009E,X024Q, X040E, X069S, X076D, X078N, X079I, X087D, X118R, X124I, X128R,X128S, X129P, X130S, X145R, X166Q, X182E, X185Q, X210I, X211P, X217L,X218S, X248D, and X259P, where the amino acid positions are numbered bycorrespondence with SEQ ID NO: 1, include variants derived fromsubtilisin polypeptides of AprE (e.g. WP_003233171); WP_082194748(formerly WP_008359041); Chemgen_164A (SEQ ID NO: 2 in U.S. Pat. No.5,275,945); CP474 (e.g. SEQ ID NO: 3 in WO2015038792); ZP-00454 (e.g.variant of WP_010192403, SEQ ID NO:7 in WO2015/038792); DSM14391 (SEQ IDNO: 13 in WO2018118917); WP_010192403 (formerly ZP 07707657 (SEQ ID NO:7 in WO2015038792)); BspZ00056 (SEQ ID NO:9 in WO 2016069544);) Bba02069(SEQ ID NO: 3 in WO2016061438); Bad02409 (SEQ ID NO: 13 in WO201069557);BspAK01305 (SEQ ID NO: 6 in WO2016069569); BspZ00258 (SEQ ID NO: 9 inWO2016069552); BspAI02518 (SEQ ID NO: 3 in WO2015089441); and Bpan01744(SEQ ID NO: 3 in WO2016069563). Other subtilisin polypeptides in whichthe disclosed substitutions find use include, but are not limited to,SEQ ID NO:7 in WO2016/001449; SEQ ID NO: 1 in WO2012/139964; SEQ ID NO:7 in WO2012/163855; SEQ ID NO: 9 in WO2016/001449; SEQ ID NO: 5 inWO2016/001449; SEQ ID NO: 6 in WO2016/001449; SEQ ID NO: 6 inWO2014/177430; SEQ ID NO: 4 in WO2011/036263; SEQ ID NO: 4 inWO2016/174234; SEQ ID NO: 7 in WO2015144932; SEQ ID NO: 119 in U.S. Pat.No. 7,981,659; SEQ ID NO: 4 in WO2016/001449; SEQ ID NO: 2 inJP2004313043; SEQ ID NO: 2 in US2015/275148; SEQ ID NO: 12 in WO201600144; SEQ ID NO: 2 in WO 2016000970; SEQ ID NO:19 in U.S. Pat. No.8,530,218; SEQ ID NO: 8 in WO 2016000973; SEQ ID NO: 8 in WO2016001449;SEQ ID NO 21 or 22 in WO2016203064 and SEQ ID NO: 21 in U.S. Pat. No.8,530,218. That is, in some embodiments, the substitutions providedherein can be used in any subtilisin having at least about 80% sequenceidentity to SEQ ID NO: 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or22. For example, subtilisins, such as SEQ ID NO 21 or 22 in WO2016203064can be engineered to include one, two, three or more additional featureswith respect to SEQ ID NO: 1 selected from a T, or V at position 3; an Eat position 9; a Q at position 24; an E at position 40; an S at position69; a D at position 76; a N at position 78; an I at position 79; a D atposition 87; an Rat position 118; an I at position 124; an R, or S atposition 128; a P at position 129; an S at position 130; an Rat position145; a Q at position 166; an E at position 182; a Q at position 185; anI at position 210; a P at position 211; an L at position 217; an S atposition 218; a D at position 248; and a P at position 259. In one suchembodiment, subtilisins, such as SEQ ID NO 21 or 22 in WO2016203064 canbe engineered to include one, two, three, four, or more, substitutionswith respect to SEQ ID NO: 1 selected from a T, or V at position 3; an Eat position 9; a Q at position 24; an E at position 40; an S at position69; a D at position 76; a N at position 78; an I at position 79; a D atposition 87; an Rat position 118; an I at position 124; an R, or S atposition 128; a P at position 129; an S at position 130; an R atposition 145; a Q at position 166; an E at position 182; a Q at position185; an I at position 210; a P at position 211; an L at position 217; anS at position 218; a D at position 248; and a P at position 259.

Still other subtilisin polypeptides in which the disclosed substitutionsfind use include, but are not limited to, those disclosed inWO_2012_175708_2; WO_2012_175708_4; U.S. Pat. No. 7,951,573 B22; U.S.Pat. No. 7,951,573 B24; U.S. Pat. No. 7,951,573 B26; U.S. Pat. No.7,951,573 B237; US7727756-0001; US9365844-0001; US7262042-0002;US20090275493-0002; US7811076-0004; US8455424-0003;WO03054184-CAE48421/SEQ ID NO: 25 in WO2015089447;WO2007131657-CA591385/SEQ ID NO:24 in WO2015089447;WO2008086916-CAV33594/SEQ ID NO:26 in WO2015089447; WO2017089162-0001;WO2017089162-0002; WO2017089162-0003; WO2017089162-0004;WO2017089162-0005; WO2017089162-0006; WO2017089162-0007;WO2017089162-0008, and WO2019180111.

In an even still further embodiment, one or more subtilisin variantsdescribed herein has improved stability, for example, improved stabilityin a detergent composition. In another embodiment, parent subtilisincomprises an amino acid sequence of SEQ ID NO: 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, or 22, or has 50%, 55%, 60%, 65%, 70%, 75%, 80%,85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or99% amino acid sequence identity to the amino acid sequence of SEQ IDNO: 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 22. In still yetanother embodiment, the stability of the one or more subtilisin variantsin detergent is measured in accordance with the stability assays ofExample 2.

In other embodiments, one or more subtilisin variants are more stablethan a reference, or parent subtilisin lacking the one, two, three ormore features. In some embodiments, such variants having increasedstability are characterized by having a Performance Index (PI) greaterthan about 1.1 with respect to a parent, or reference, protease after 20minutes incubation in 10% liquid detergent at 30-70 degrees Celsius. Insome embodiments, the reference subtilisin refers to a subtilisin havingthe highest identity to the variant subtilisin, but not containing therecited features.

One or more subtilisin variants described herein can be subject tovarious changes, such as one or more amino acid insertion, deletion,and/or substitution, either conservative or non-conservative, includingwhere such changes do not substantially alter the enzymatic activity ofthe variant. Similarly, a polynucleotide encoding the subtilisin variantof the invention can also be subject to various changes, such as one ormore substitution of one or more nucleotide in one or more codon suchthat a particular codon encodes the same or a different amino acid,resulting in either a silent variation (e.g., when the encoded aminoacid is not altered by the nucleotide mutation) or non-silent variation;one or more deletion of one or more nucleotides (or codon) in thesequence; one or more addition or insertion of one or more nucleotides(or codon) in the sequence; and/or cleavage of, or one or moretruncation, of one or more nucleotides (or codon) in the sequence. Manysuch changes in the nucleic acid sequence may not substantially alterthe enzymatic activity of the resulting encoded polypeptide enzymecompared to the polypeptide enzyme encoded by the original nucleic acidsequence. A nucleic acid sequence described herein can also be modifiedto include one or more codon that provides for optimum expression in anexpression system (e.g., bacterial expression system), while, ifdesired, said one or more codon still encodes the same amino acid(s).

Described herein is one or more isolated, non-naturally occurring, orrecombinant polynucleotide comprising a nucleic acid sequence thatencodes one or more subtilisin variants described herein, or recombinantpolypeptide or active fragment thereof. One or more nucleic acidsequence described herein is useful in recombinant production (e.g.,expression) of one or more subtilisin variants described herein, forexample, through expression of a plasmid expression vector comprising asequence encoding the one or more subtilisin variants described hereinor fragment thereof. One embodiment provides nucleic acids encoding oneor more subtilisin variants described herein, wherein the variant is amature form having proteolytic activity. In some embodiments, one ormore subtilisin variants described herein is expressed recombinantlywith a homologous pro-peptide sequence. In other embodiments, one ormore subtilisin variants described herein is expressed recombinantlywith a heterologous pro-peptide sequence (e.g., pro-peptide sequencefrom B. lentus).

One or more nucleic acid sequence described herein can be generated byusing any suitable synthesis, manipulation, and/or isolation techniques,or combinations thereof. For example, one or more polynucleotidedescribed herein may be produced using standard nucleic acid synthesistechniques, such as solid-phase synthesis techniques that are well-knownto those skilled in the art. In such techniques, fragments of up to 50or more nucleotide bases are typically synthesized, then joined (e.g.,by enzymatic or chemical ligation methods) to form essentially anydesired continuous nucleic acid sequence. The synthesis of the one ormore polynucleotide described herein can be also facilitated by anysuitable method known in the art, including but not limited to chemicalsynthesis using the classical phosphoramidite method (See e.g., Beaucageet al. Tetrahedron Letters 22:1859-69 (1981)), or the method describedin Matthes et al., EMBO J. 3:801-805 (1984) as is typically practiced inautomated synthetic methods. One or more polynucleotide described hereincan also be produced by using an automatic DNA synthesizer. Customizednucleic acids can be ordered from a variety of commercial sources (e.g.,ATUM (DNA 2.0), Newark, Calif., USA; Life Tech (GeneArt), Carlsbad,Calif., USA; GenScript, Ontario, Canada; Base Clear B. V., Leiden,Netherlands; Integrated DNA Technologies, Skokie, Ill., USA; GinkgoBioworks (Gen9), Boston, Mass., USA; and Twist Bioscience, SanFrancisco, Calif., USA). Other techniques for synthesizing nucleic acidsand related principles are described by, for example, Itakura et al.,Ann. Rev. Biochem. 53:323 (1984) and Itakura et al., Science 198:1056(1984).

Recombinant DNA techniques useful in modification of nucleic acids arewell known in the art, such as, for example, restriction endonucleasedigestion, ligation, reverse transcription and cDNA production, andpolymerase chain reaction (e.g., PCR). One or more polynucleotidedescribed herein may also be obtained by screening cDNA libraries usingone or more oligonucleotide probes that can hybridize to or PCR-amplifypolynucleotides which encode one or more subtilisin variant describedherein, or recombinant polypeptide or active fragment thereof.Procedures for screening and isolating cDNA clones and PCR amplificationprocedures are well known to those of skill in the art and described instandard references known to those skilled in the art. One or morepolynucleotide described herein can be obtained by altering a naturallyoccurring polynucleotide backbone (e.g., that encodes one or moresubtilisin variant described herein or reference subtilisin) by, forexample, a known mutagenesis procedure (e.g., site-directed mutagenesis,site saturation mutagenesis, and in vitro recombination). A variety ofmethods are known in the art that are suitable for generating modifiedpolynucleotides described herein that encode one or more subtilisinvariant described herein, including, but not limited to, for example,site-saturation mutagenesis, scanning mutagenesis, insertionalmutagenesis, deletion mutagenesis, random mutagenesis, site-directedmutagenesis, and directed-evolution, as well as various otherrecombinatorial approaches.

A further embodiment is directed to one or more vector comprising one ormore subtilisin variant described herein (e.g., a polynucleotideencoding one or more subtilisin variant described herein); expressionvectors or expression cassettes comprising one or more nucleic acid orpolynucleotide sequence described herein; isolated, substantially pure,or recombinant DNA constructs comprising one or more nucleic acid orpolynucleotide sequence described herein; isolated or recombinant cellscomprising one or more polynucleotide sequence described herein; andcompositions comprising one or more such vector, nucleic acid,expression vector, expression cassette, DNA construct, cell, cellculture, or any combination or mixtures thereof.

Some embodiments are directed to one or more recombinant cell comprisingone or more vector (e.g., expression vector or DNA construct) describedherein which comprises one or more nucleic acid or polynucleotidesequence described herein. Some such recombinant cells are transformedor transfected with such at least one vector, although other methods areavailable and known in the art. Such cells are typically referred to ashost cells. Some such cells comprise bacterial cells, including, but notlimited to Bacillus sp. cells, such as B. subtilis cells. Otherembodiments are directed to recombinant cells (e.g., recombinant hostcells) comprising one or more subtilisin described herein.

In some embodiments, one or more vector described herein is anexpression vector or expression cassette comprising one or morepolynucleotide sequence described herein operably linked to one or moreadditional nucleic acid segments required for efficient gene expression(e.g., a promoter operably linked to one or more polynucleotide sequencedescribed herein). A vector may include a transcription terminatorand/or a selection gene (e.g., an antibiotic resistance gene) thatenables continuous cultural maintenance of plasmid-infected host cellsby growth in antimicrobial-containing media.

An expression vector may be derived from plasmid or viral DNA, or inalternative embodiments, contains elements of both. Exemplary vectorsinclude, but are not limited to pC194, pJH101, pE194, pHP13 (See,Harwood and Cutting [eds.], Chapter 3, Molecular Biological Methods forBacillus, John Wiley & Sons (1990); suitable replicating plasmids for B.subtilis include those listed on p. 92). (See also, Perego,“Integrational Vectors for Genetic Manipulations in Bacillus subtilis”;Sonenshein et al., [eds.]; “Bacillus subtilis and Other Gram-PositiveBacteria: Biochemistry, Physiology and Molecular Genetics”, AmericanSociety for Microbiology, Washington, D.C. (1993), pp. 615-624); andp2JM103BBI).

For expression and production of a protein of interest (e.g., one ormore subtilisin variant described herein) in a cell, one or moreexpression vector comprising one or more copy of a polynucleotideencoding one or more subtilisin variant described herein, and in someinstances comprising multiple copies, is transformed into the cell underconditions suitable for expression of the variant. In some embodiments,a polynucleotide sequence encoding one or more subtilisin variantdescribed herein (as well as other sequences included in the vector) isintegrated into the genome of the host cell, while in other embodiments,a plasmid vector comprising a polynucleotide sequence encoding one ormore subtilisin variant described herein remains as autonomousextra-chromosomal element within the cell. Some embodiments provide bothextrachromosomal nucleic acid elements as well as incoming nucleotidesequences that are integrated into the host cell genome. The vectorsdescribed herein are useful for production of the one or more subtilisinvariant described herein. In some embodiments, a polynucleotideconstruct encoding one or more subtilisin variant described herein ispresent on an integrating vector that enables the integration andoptionally the amplification of the polynucleotide encoding the variantinto the host chromosome. Examples of sites for integration are wellknown to those skilled in the art. In some embodiments, transcription ofa polynucleotide encoding one or more subtilisin variant describedherein is effectuated by a promoter that is the wildtype promoter forthe parent subtilisin. In some other embodiments, the promoter isheterologous to the one or more subtilisin variant described herein, butis functional in the host cell. Exemplary promoters for use in bacterialhost cells include, but are not limited to the amyE, amyQ, amyL, pstS,sacB, pSPAC, pAprE, pVeg, pHpaII promoters; the promoter of the B.stearothermophilus maltogenic amylase gene; the B. amyloliquefaciens(BAN) amylase gene; the B. subtilis alkaline protease gene; the B.clausii alkaline protease gene; the B. pumilis xylosidase gene; the B.thuringiensis cryIIIA; and the B. licheniformis alpha-amylase gene.Additional promoters include, but are not limited to the A4 promoter, aswell as phage Lambda PR or PL promoters and the E. coli lac, trp or tacpromoters.

One or more subtilisin variant described herein can be produced in hostcells of any suitable microorganism, including bacteria and fungi. Insome embodiments, one or more subtilisin variant described herein can beproduced in Gram-positive bacteria. In some embodiments, the host cellsare Bacillus spp., Streptomyces spp., Escherichia spp., Aspergillusspp., Trichoderma spp., Pseudomonas spp., Corynebacterium spp.,Saccharomyces spp., or Pichia spp. In some embodiments, one or moresubtilisin variant described herein is produced by Bacillus sp. hostcells. Examples of Bacillus sp. host cells that find use in theproduction of the one or more subtilisin variant described hereininclude, but are not limited to B. licheniformis, B. lentus, B.subtilis, B. amyloliquefaciens, B. brevis, B. stearothermophilus, B.alkalophilus, B. coagulans, B. circulans, B. pumilis, B. thuringiensis,B. clausii, and B. megaterium, as well as other organisms within thegenus Bacillus. In some embodiments, B. subtilis host cells are used toproduce the variants described herein. U.S. Pat. Nos. 5,264,366 and4,760,025 (RE 34,606) describe various Bacillus host strains that can beused to produce one or more subtilisin variant described herein,although other suitable strains can be used.

Several bacterial strains that can be used to produce one or moresubtilisin variant described herein include non-recombinant (i.e.,wildtype) Bacillus sp. strains, as well as variants ofnaturally-occurring strains and/or recombinant strains. In someembodiments, the host strain is a recombinant strain, wherein apolynucleotide encoding one or more subtilisin variant described hereinhas been introduced into the host. In some embodiments, the host strainis a B. subtilis host strain and particularly a recombinant B. subtilishost strain. Numerous B. subtilis strains are known, including, but notlimited to for example, 1A6 (ATCC 39085), 168 (1A01), SB19, W23, Ts85,B637, PB1753 through PB1758, PB3360, JH642, 1A243 (ATCC 39,087), ATCC21332, ATCC 6051, MI113, DE100 (ATCC 39,094), GX4931, PBT 110, and PEP211strain (See e.g., Hoch et al., Genetics 73:215-228 (1973); See also,U.S. Pat. Nos. 4,450,235; 4,302,544; and EP 0134048). The use of B.subtilis as an expression host cell is well known in the art (See e.g.,Palva et al., Gene 19:81-87 (1982); Fahnestock and Fischer, J.Bacteriol., 165:796-804 (1986); and Wang et al., Gene 69:39-47 (1988)).

In some embodiments, the Bacillus host cell is a Bacillus sp. thatincludes a mutation or deletion in at least one of the following genes:degU, degS, degR and degQ. In some embodiments, the mutation is in adegU gene, and in some embodiments the mutation is degU(Hy)32 (See e.g.,Msadek et al., J. Bacteriol. 172:824-834 (1990); and Olmos et al., Mol.Gen. Genet. 253:562-567 (1997)). In some embodiments, the Bacillus hostcomprises a mutation or deletion in scoC4 (See e.g., Caldwell et al., J.Bacteriol. 183:7329-7340 (2001)); spoIIE (See e.g., Arigoni et al., Mol.Microbiol. 31:1407-1415 (1999)); and/or oppA or other genes of the oppoperon (See e.g., Perego et al., Mol. Microbiol. 5:173-185 (1991)).Indeed, it is contemplated that any mutation in the opp operon thatcauses the same phenotype as a mutation in the oppA gene will find usein some embodiments of the altered Bacillus strain described herein. Insome embodiments, these mutations occur alone, while in otherembodiments, combinations of mutations are present. In some embodiments,an altered Bacillus host cell strain that can be used to produce one ormore subtilisin variant described herein is a Bacillus host strain thatalready includes a mutation in one or more of the above-mentioned genes.In addition, Bacillus sp. host cells that comprise mutation(s) and/ordeletion(s) of endogenous protease genes find use. In some embodiments,the Bacillus host cell comprises a deletion of the aprE and the nprEgenes. In other embodiments, the Bacillus sp. host cell comprises adeletion of 5 protease genes, while in other embodiments the Bacillussp. host cell comprises a deletion of 9 protease genes (See e.g., US2005/0202535).

Host cells are transformed with one or more nucleic acid sequenceencoding one or more subtilisin variant described herein using anysuitable method known in the art. Methods for introducing a nucleic acid(e.g., DNA) into Bacillus cells or E. coli cells utilizing plasmid DNAconstructs or vectors and transforming such plasmid DNA constructs orvectors into such cells are well known. In some embodiments, theplasmids are subsequently isolated from E. coli cells and transformedinto Bacillus cells. However, it is not essential to use interveningmicroorganisms such as E. coli, and in some embodiments, a DNA constructor vector is directly introduced into a Bacillus host.

Exemplary methods for introducing one or more nucleic acid sequencedescribed herein into Bacillus cells are described in, for example,Ferrari et al., “Genetics,” in Harwood et al. [eds.], Bacillus, PlenumPublishing Corp. (1989), pp. 57-72; Saunders et al., J. Bacteriol.157:718-726 (1984); Hoch et al., J. Bacteriol. 93:1925-1937 (1967); Mannet al., Current Microbiol. 13:131-135 (1986); Holubova, Folia Microbiol.30:97 (1985); Chang et al., Mol. Gen. Genet. 168:11-115 (1979);Vorobjeva et al., FEMS Microbiol. Lett. 7:261-263 (1980); Smith et al.,Appl. Env. Microbiol. 51:634 (1986); Fisher et al., Arch. Microbiol.139:213-217 (1981); and McDonald, J. Gen. Microbiol. 130:203 (1984)).Indeed, such methods as transformation, including protoplasttransformation and transfection, transduction, and protoplast fusion arewell known and suited for use herein. Methods known in the art totransform Bacillus cells include such methods as plasmid marker rescuetransformation, which involves the uptake of a donor plasmid bycompetent cells carrying a partially homologous resident plasmid (See,Contente et al., Plasmid 2:555-571 (1979); Haima et al., Mol. Gen.Genet. 223:185-191 (1990); Weinrauch et al., J. Bacteriol. 154:1077-1087(1983); and Weinrauch et al., J. Bacteriol. 169:1205-1211 (1987)). Inthis method, the incoming donor plasmid recombines with the homologousregion of the resident “helper” plasmid in a process that mimicschromosomal transformation.

In addition to commonly used methods, in some embodiments, host cellsare directly transformed with a DNA construct or vector comprising anucleic acid encoding one or more subtilisin variant described herein(i.e., an intermediate cell is not used to amplify, or otherwiseprocess, the DNA construct or vector prior to introduction into the hostcell). Introduction of a DNA construct or vector described herein intothe host cell includes those physical and chemical methods known in theart to introduce a nucleic acid sequence (e.g., DNA sequence) into ahost cell without insertion into the host genome. Such methods include,but are not limited to calcium chloride precipitation, electroporation,naked DNA, and liposomes. In additional embodiments, DNA constructs orvector are co-transformed with a plasmid, without being inserted intothe plasmid. In further embodiments, a selective marker is deleted fromthe altered Bacillus strain by methods known in the art (See, Stahl etal., J. Bacteriol. 158:411-418 (1984); and Palmeros et al., Gene247:255-264 (2000)).

In some embodiments, the transformed cells are cultured in conventionalnutrient media. The suitable specific culture conditions, such astemperature, pH and the like are known to those skilled in the art andare well described in the scientific literature. Some embodimentsprovide a culture (e.g., cell culture) comprising one or more subtilisinvariant or nucleic acid sequence described herein.

In some embodiments, host cells transformed with one or morepolynucleotide sequence encoding one or more subtilisin variantdescribed herein are cultured in a suitable nutrient medium underconditions permitting the expression of the variant, after which theresulting variant is recovered from the culture. In some embodiments,the variant produced by the cells is recovered from the culture mediumby conventional procedures, including, but not limited to, for example,separating the host cells from the medium by centrifugation orfiltration, precipitating the proteinaceous components of thesupernatant or filtrate by means of a salt (e.g., ammonium sulfate), andchromatographic purification (e.g., ion exchange, gel filtration,affinity, etc.).

In some embodiments, one or more subtilisin variant produced by arecombinant host cell is secreted into the culture medium. A nucleicacid sequence that encodes a purification facilitating domain may beused to facilitate purification of the variant. A vector or DNAconstruct comprising a polynucleotide sequence encoding one or moresubtilisin variant described herein may further comprise a nucleic acidsequence encoding a purification facilitating domain to facilitatepurification of the variant (See e.g., Kroll et al., DNA Cell Biol.12:441-53 (1993)). Such purification facilitating domains include, butare not limited to, for example, metal chelating peptides such ashistidine-tryptophan modules that allow purification on immobilizedmetals (See, Porath, Protein Expr. Purif. 3:263-281 [1992]), protein Adomains that allow purification on immobilized immunoglobulin, and thedomain utilized in the FLAGS extension/affinity purification system. Theinclusion of a cleavable linker sequence such as Factor XA orenterokinase (e.g., sequences available from Invitrogen, San Diego,Calif.) between the purification domain and the heterologous proteinalso find use to facilitate purification.

A variety of methods can be used to determine the level of production ofone or more mature subtilisin variant described herein in a host cell.Such methods include, but are not limited to, for example, methods thatutilize either polyclonal or monoclonal antibodies specific for theprotease. Exemplary methods include, but are not limited toenzyme-linked immunosorbent assays (ELISA), radioimmunoassays (MA),fluorescent immunoassays (FIA), and fluorescent activated cell sorting(FACS). These and other assays are well known in the art (See e.g.,Maddox et al., J. Exp. Med. 158:1211 (1983)).

Some other embodiments provide methods for making or producing one ormore mature subtilisin variant described herein. A mature subtilisinvariant does not include a signal peptide or a propeptide sequence. Somemethods comprise making or producing one or more subtilisin variantdescribed herein in a recombinant bacterial host cell, such as forexample, a Bacillus sp. cell (e.g., a B. subtilis cell). Otherembodiments provide a method of producing one or more subtilisin variantdescribed herein, wherein the method comprises cultivating a recombinanthost cell comprising a recombinant expression vector comprising anucleic acid sequence encoding one or more subtilisin variant describedherein under conditions conducive to the production of the variant. Somesuch methods further comprise recovering the variant from the culture.

Further embodiments provide methods of producing one or more subtilisinvariant described herein, wherein the methods comprise: (a) introducinga recombinant expression vector comprising a nucleic acid encoding thevariant into a population of cells (e.g., bacterial cells, such as B.subtilis cells); and (b) culturing the cells in a culture medium underconditions conducive to produce the variant encoded by the expressionvector. Some such methods further comprise: (c) isolating the variantfrom the cells or from the culture medium.

Unless otherwise noted, all component or composition levels providedherein are made in reference to the active level of that component orcomposition, and are exclusive of impurities, for example, residualsolvents or by-products, which may be present in commercially availablesources. Enzyme components weights are based on total active protein.All percentages and ratios are calculated by weight unless otherwiseindicated. All percentages and ratios are calculated based on the totalcomposition unless otherwise indicated. Compositions described hereininclude cleaning compositions, such as detergent compositions. In theexemplified detergent compositions, the enzyme levels are expressed bypure enzyme by weight of the total composition and unless otherwisespecified, the detergent ingredients are expressed by weight of thetotal compositions.

The subtilisin variants provided herein may be used in the production ofvarious compositions, such as enzyme compositions and cleaning ordetergent compositions. An enzyme composition comprises a subtilisinvariant as provided herein. The enzyme composition can be in any form,such as granule, liquid formulations, or enzyme slurries.

Enzyme granules may be made by, e.g., rotary atomization, wetgranulation, dry granulation, spray drying, disc granulation, extrusion,pan coating, spheronization, drum granulation, fluid-bed agglomeration,high-shear granulation, fluid-bed spray coating, crystallization,precipitation, emulsion gelation, spinning disc atomization and othercasting approaches, and prilling processes. The core of the granule maybe the granule itself or the inner nucleus of a layered granule.

The core may comprise one or more water soluble or dispersible agent(s),including but not limited to, sodium sulfate, sodium chloride, magnesiumsulfate, zinc sulfate, and ammonium sulfate), citric acid, sugars (e.g.,sucrose, lactose, glucose, granulated sucrose, maltodextrin andfructose), plasticizers (e.g., polyols, urea, dibutyl phthalate, anddimethyl phthalate), fibrous material (e.g., cellulose and cellulosederivatives such as hydroxyl-propyl-methyl cellulose, carboxy-methylcellulose, and hydroxyl-ethyl cellulose), phosphate, calcium, a proteaseinhibitor and combinations thereof. Suitable dispersible agents include,but are not limited to, clays, nonpareils (combinations of sugar andstarch; e.g., starch-sucrose non-pareils-ASNP), talc, silicates,carboxymethyl cellulose, starch, and combinations thereof.

In some embodiments, the core comprises mainly sodium sulfate. In someembodiments, the core consists essentially of sodium sulfate. In aparticular embodiment, the core consists of only sodium sulfate.

In some embodiments, the core comprises a subtilisin variant as providedherein. In other embodiments, the core comprises one or more enzymes inaddition to protease. In other embodiments, the core is inert and doesnot comprise enzymes.

In some embodiments, the core is an enzyme powder, including UFCcontaining an enzyme. The enzyme powder may be spray dried and mayoptionally be admixed with any of the water soluble or dispersibleagents listed, herein. The enzyme may be, or may include, the proteaseto be stabilized, in which case the enzyme power should further includea stabilizer.

In some embodiments the core is coated with at least one coating layer.In a particular embodiment, the core is coated with at least two coatinglayers. In another particular embodiment the core is coated with atleast three coating layers. The materials used in the coating layer(s)can be suitable for use in cleaning and/or detergent compositions.

In some embodiments, a coating layer comprises one of more of thefollowing materials: an inorganic salt (e.g., sodium sulfate, sodiumchloride, magnesium sulfate, zinc sulfate, and ammonium sulfate), citricacid, a sugar (e.g., sucrose, lactose, glucose, and fructose), aplasticizer (e.g., polyols, urea, dibutyl phthalate, and dimethylphthalate), fibrous material (e.g., cellulose and cellulose derivativessuch as hydroxyl-propyl-methyl cellulose, carboxy-methyl cellulose, andhydroxyl-ethyl cellulose), clay, nonpareil (a combination of sugar andstarch), silicate, carboxymethyl cellulose, phosphate, starch (e.g.,corn starch), fats, oils (e.g., rapeseed oil, and paraffin oil), lipids,vinyl polymers, vinyl copolymers, polyvinyl alcohol (PVA), plasticizers(e.g., polyols, urea, dibutyl phthalate, dimethyl phthalate, and water),anti-agglomeration agents (e.g., talc, clays, amorphous silica, andtitanium dioxide), anti-foam agents (such as FOAMBLAST 882® and EROL6000K®), and talc. US20100124586, WO9932595, and U.S. Pat. No. 5,324,649detail suitable components for the coating layers.

In some embodiments, the coating layer comprises sugars (e.g., sucrose,lactose, glucose, granulated sucrose, maltodextrin and fructose). Insome embodiments, the coating layer comprises a polymer such aspolyvinyl alcohol (PVA). Suitable PVA for incorporation in the coatinglayer(s) of the multi-layered granule include partially hydrolyzed,fully hydrolyzed and intermediately hydrolyzed having low to highdegrees of viscosity. In some embodiments, the coating layer comprisesan inorganic salt, such as sodium sulfate.

In some embodiments, at least one coating layer is an enzyme coatinglayer. In some embodiments the core is coated with at least two enzymelayers. In another embodiment the core is coated with at least three ormore enzyme layers.

In some embodiments, the enzymes are protease in combination with one ormore additional enzymes selected from the group consisting of acyltransferases, alpha-amylases, beta-amylases, alpha-galactosidases,arabinosidases, aryl esterases, beta-galactosidases, carrageenases,catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases,endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases,exo-mannanases, galactanases, glucoamylases, hemicellulases,hyaluronidases, keratinases, laccases, lactases, ligninases, lipases,lipoxygenases, mannanases, metalloproteases, nucleases (e.g. DNasesand/or RNases), oxidases, oxidoreductases, pectate lyases, pectin acetylesterases, pectinases, pentosanases, perhydrolases, peroxidases,phenoloxidases, phosphatases, phospholipases, phytases,polygalacturonases, polyesterases, additional proteases, pullulanases,reductases, rhamnogalacturonases, beta-glucanases, tannases,transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases,xylosidases, and any combination or mixture thereof. Generally, at leastone enzyme coating layer comprises at least one protease.

The above enzyme lists are examples only and are not meant to beexclusive. Any enzyme can be used in the granules described herein,including wild type, recombinant and variant enzymes of bacterial,fungal, yeast sources, and acid, neutral or alkaline enzymes.

In one embodiment, one or more subtilisin variant described herein isuseful in cleaning applications, such as, for example, but not limitedto, cleaning dishware or tableware items, fabrics, medical instrumentsand items having hard surfaces (e.g., the hard surface of a table, tabletop, wall, furniture item, floor, and ceiling). In other embodiments,one or more subtilisin variant described herein is useful indisinfecting applications, such as, for example, but not limited to,disinfecting an automatic dishwashing or laundry machine. In otherembodiments, one or more subtilisin variant described herein andcompositions comprising such variant are useful in applications toremove or prevent malodor, such as, for example, but not limited to, onlaundry, hard surfaces, automatic dishwashing or laundry machines.

Another embodiment is directed to a composition comprising one or moresubtilisin variant described herein. In some embodiments, thecomposition is a cleaning composition. In other embodiments, thecomposition is a detergent composition. In yet other embodiments, thecomposition is selected from a laundry detergent composition, anautomatic dishwashing (ADW) composition, a hand (manual) dishwashingdetergent composition, a hard surface cleaning composition, an eyeglasscleaning composition, a medical instrument cleaning composition, adisinfectant (e.g., malodor or microbial) composition, and a personalcare cleaning composition. In still other embodiments, the compositionis a laundry detergent composition, an ADW composition, or a hand(manual) dishwashing detergent composition. Even still furtherembodiments are directed to fabric cleaning compositions, while otherembodiments are directed to non-fabric cleaning compositions. In someembodiments, the cleaning composition is boron-free. In otherembodiments, the cleaning composition is phosphate-free. In still otherembodiments, the composition comprises one or more subtilisin variantdescribed herein and one or more of an excipient, adjunct material,and/or additional enzyme.

In yet still a further embodiment, the composition described hereincontains phosphate, is phosphate-free, contains boron, is boron-free, orcombinations thereof. In other embodiments, the composition is aboron-free composition. In some embodiments, a boron-free composition isa composition to which a borate stabilizer has not been added. Inanother embodiment, a boron-free composition is a composition thatcontains less than 5.5% boron. In a still further embodiment, aboron-free composition is a composition that contains less than 4.5%boron. In yet still another embodiment, a boron-free composition is acomposition that contains less than 3.5% boron. In yet still a furtherembodiment, a boron-free composition is a composition that contains lessthan 2.5% boron. In even further embodiments, a boron-free compositionis a composition that contains less than 1.5% boron. In anotherembodiment, a boron-free composition is a composition that contains lessthan 1.0% boron. In still further embodiments, a boron-free compositionis a composition that contains less than 0.5% boron. In still furtherembodiments, a boron-free composition is a composition substantiallyfree of boron. In other embodiments, the composition is a compositionfree or substantially free of enzyme stabilizers or peptide inhibitors.

In another embodiment, one or more composition described herein is in aform selected from gel, tablet, powder, granular, solid, liquid, unitdose, and combinations thereof. In yet another embodiment, one or morecomposition described herein is in a form selected from a low watercompact formula, low water HDL or Unit Dose (UD), or high water formulaor HDL. In some embodiments, the cleaning composition described hereinis in a unit dose form. In other embodiments, the unit dose form isselected from pills, tablets, capsules, gelcaps, sachets, pouches,multi-compartment pouches, and pre-measured powders or liquids. In someembodiments, the unit dose format is designed to provide controlledrelease of the ingredients within a multi-compartment pouch (or otherunit dose format). Suitable unit dose and controlled release formats aredescribed, for example, in EP 2100949; WO 02/102955; U.S. Pat. Nos.4,765,916; 4,972,017; and WO 04/111178. In some embodiments, the unitdose form is a tablet or powder contained in a water-soluble film orpouch.

Exemplary laundry detergent compositions include, but are not limitedto, for example, liquid and powder laundry detergent compositions.Exemplary hard surface cleaning compositions include, but are notlimited to, for example, compositions used to clean the hard surface ofa non-dishware item, non-tableware item, table, table top, furnitureitem, wall, floor, and ceiling. Exemplary hard surface cleaningcompositions are described, for example, in U.S. Pat. Nos. 6,610,642,6,376,450, and 6,376,450. Exemplary personal care compositions include,but are not limited to, compositions used to clean dentures, teeth,hair, contact lenses, and skin. Exemplary components of such oral carecomposition include those described in, for example, U.S. Pat. No.6,376,450.

In some embodiments, one or more subtilisin variant described hereincleans at low temperatures. In other embodiments, one or morecomposition described herein cleans at low temperatures. In otherembodiments, one or more composition described herein comprises aneffective amount of one or more subtilisin variant described herein asuseful or effective for cleaning a surface in need of proteinaceousstain removal.

In some embodiments, adjunct materials are incorporated, for example, toassist or enhance cleaning performance; for treatment of the substrateto be cleaned; or to modify the aesthetics of the cleaning compositionas is the case with perfumes, colorants, dyes or the like. Oneembodiment is directed to a composition comprising one or more adjunctmaterial and one or more subtilisin variant described herein. Anotherembodiment is directed to a composition comprising one or more adjunctmaterial and one or more subtilisin variant described herein, whereinthe adjunct material is selected from a bleach catalyst, an additionalenzyme, an enzyme stabilizer (including, for example, an enzymestabilizing system), a chelant, an optical brightener, a soil releasepolymer, a dye transfer agent, a dispersant, a suds suppressor, a dye, aperfume, a colorant, a filler, a photoactivator, a fluorescer, a fabricconditioner, a hydrolyzable surfactant, a preservative, an anti-oxidant,an anti-shrinkage agent, an anti-wrinkle agent, a germicide, afungicide, a color speckle, a silvercare agent, an anti-tarnish agent,an anti-corrosion agent, an alkalinity source, a solubilizing agent, acarrier, a processing aid, a pigment, a pH control agent, a surfactant,a builder, a chelating agent, a dye transfer inhibiting agent, adeposition aid, a catalytic material, a bleach activator, a bleachbooster, a hydrogen peroxide, a source of hydrogen peroxide, a preformedperacid, a polymeric dispersing agent, a clay soilremoval/anti-redeposition agent, a structure elasticizing agent, afabric softener, a carrier, a hydrotrope, a processing aid, a pigment,and combinations thereof. Exemplary adjunct materials and levels of useare found in U.S. Pat. Nos. 5,576,282; 6,306,812; 6,326,348; 6,610,642;6,605,458; 5,705,464; 5,710,115; 5,698,504; 5,695,679; 5,686,014 and5,646,101. In embodiments in which one or more cleaning adjunct materialis not compatible with one or more subtilisin variant described herein,methods are employed to keep the adjunct material and variant(s)separated (i.e., not in contact with each other) until combination ofthe two components is appropriate. Such separation methods include anysuitable method known in the art (e.g., gelcaps, encapsulation, tablets,physical separation, etc.).

Some embodiments are directed to cleaning additive products comprisingone or more subtilisin variant described herein. In some embodiments,the additive is packaged in a dosage form for addition to a cleaningprocess. In some embodiments, the additive is packaged in a dosage formfor addition to a cleaning process where a source of peroxygen isemployed and increased bleaching effectiveness is desired.

Exemplary fillers or carriers for granular compositions include, but arenot limited to, for example, various salts of sulfate, carbonate andsilicate; talc; and clay. Exemplary fillers or carriers for liquidcompositions include, but are not limited to, for example, water or lowmolecular weight primary and secondary alcohols including polyols anddiols (e.g., methanol, ethanol, propanol and isopropanol). In someembodiments, the compositions contain from about 5% to about 90% of suchfiller or carrier. Acidic fillers may be included in such compositionsto reduce the pH of the resulting solution in the cleaning method orapplication.

In one embodiment, one or more cleaning composition described hereincomprises an effective amount of one or more subtilisin variantdescribed herein, alone or in combination with one or more additionalenzyme. Typically, a cleaning composition comprises at least about0.0001 to about 20 wt %, from about 0.0001 to about 10 wt %, from about0.0001 to about 1 wt %, from about 0.001 to about 1 wt %, or from about0.01 to about 0.1 wt % of one or more protease. In another embodiment,one or more cleaning composition described herein comprises from about0.01 to about 10 mg, about 0.01 to about 5 mg, about 0.01 to about 2 mg,about 0.01 to about 1 mg, about 0.05 to about 1 mg, about 0.5 to about10 mg, about 0.5 to about 5 mg, about 0.5 to about 4 mg, about 0.5 toabout 3 mg, about 0.5 to about 2 mg, about 0.5 to about 1 mg, about 0.1to about 10 mg, about 0.1 to about 5 mg, about 0.1 to about 4 mg, about0.1 to about 3 mg, about 0.1 to about 2 mg, about 0.1 to about 1 mg, orabout 0.1 to about 0.5 mg of one or more protease per gram ofcomposition.

The cleaning compositions described herein are typically formulated suchthat during use in aqueous cleaning operations, the wash water will havea pH of from about 4.0 to about 11.5, or even from about 5.0 to about11.5, or even from about 5.0 to about 8.0, or even from about 7.5 toabout 10.5. Liquid product formulations are typically formulated to havea pH from about 3.0 to about 9.0 or even from about 3 to about 5.Granular laundry products are typically formulated to have a pH fromabout 8 to about 11. In some embodiments, the cleaning compositions ofthe present invention can be formulated to have an alkaline pH underwash conditions, such as a pH of from about 8.0 to about 12.0, or fromabout 8.5 to about 11.0, or from about 9.0 to about 11.0. In someembodiments, the cleaning compositions of the present invention can beformulated to have a neutral pH under wash conditions, such as a pH offrom about 5.0 to about 8.0, or from about 5.5 to about 8.0, or fromabout 6.0 to about 8.0, or from about 6.0 to about 7.5. In someembodiments, the neutral pH conditions can be measured when the cleaningcomposition is dissolved 1:100 (wt:wt) in de-ionised water at 20° C.,measured using a conventional pH meter. Techniques for controlling pH atrecommended usage levels include the use of buffers, alkalis, acids,etc., and are well known to those skilled in the art.

In some embodiments, one or more subtilisin variant described herein isencapsulated to protect it during storage from the other components inthe composition and/or control the availability of the variant duringcleaning. In some embodiments, encapsulation enhances the performance ofthe variant and/or additional enzyme. In some embodiments, theencapsulating material typically encapsulates at least part of thesubtilisin variant described herein. Typically, the encapsulatingmaterial is water-soluble and/or water-dispersible. In some embodiments,the encapsulating material has a glass transition temperature (Tg) of 0°C. or higher. Exemplary encapsulating materials include, but are notlimited to, carbohydrates, natural or synthetic gums, chitin, chitosan,cellulose and cellulose derivatives, silicates, phosphates, borates,polyvinyl alcohol, polyethylene glycol, paraffin waxes, and combinationsthereof. When the encapsulating material is a carbohydrate, it istypically selected from monosaccharides, oligosaccharides,polysaccharides, and combinations thereof. In some embodiments, theencapsulating material is a starch (See e.g., EP0922499, U.S. Pat. Nos.4,977,252, 5,354,559, and 5,935,826). In some embodiments, theencapsulating material is a microsphere made from plastic such asthermoplastics, acrylonitrile, methacrylonitrile, polyacrylonitrile,polymethacrylonitrile and mixtures thereof. Exemplary commercialmicrospheres include, but are not limited to EXPANCEL® (Stockviksverken,Sweden); and PM 6545, PM 6550, PM 7220, PM 7228, EXTENDOSPHERES®,LUXSIL®, Q-CEL®, and SPHERICEL® (PQ Corp., Valley Forge, Pa.).

There are a variety of wash conditions including varying detergentformulations, wash water volumes, wash water temperatures, and lengthsof wash time to which one or more subtilisin variant described hereinmay be exposed. A low detergent concentration system is directed to washwater containing less than about 800 ppm detergent components. A mediumdetergent concentration system is directed to wash containing betweenabout 800 ppm and about 2000 ppm detergent components. A high detergentconcentration system is directed to wash water containing greater thanabout 2000 ppm detergent components. In some embodiments, the “coldwater washing” of the present invention utilizes “cold water detergent”suitable for washing at temperatures from about 10° C. to about 40° C.,from about 20° C. to about 30° C., or from about 15° C. to about 25° C.,as well as all other combinations within the range of about 15° C. toabout 35° C. or 10° C. to 40° C.

Different geographies have different water hardness. Hardness is ameasure of the amount of calcium (Ca²⁺) and magnesium (Mg²⁺) in thewater. Water hardness is usually described in terms of the grains pergallon (gpg) mixed Ca²⁺/Mg²⁺. Most water in the United States is hard,but the degree of hardness varies. Moderately hard (60-120 ppm) to hard(121-181 ppm) water has 60 to 181 ppm (ppm can be converted to grainsper U.S. gallon by dividing ppm by 17.1) of hardness minerals.

Water Grains per gallon Parts per million Soft less than 1.0 less than17 Slightly hard 1.0 to 3.5 17 to 60 Moderately hard 3.5 to 7.0 60 to120 Hard 7.0 to 10.5 120 to 180 Very hard greater than 10.5 greater than180

Other embodiments are directed to one or more cleaning compositioncomprising from about 0.00001% to about 10% by weight composition of oneor more subtilisin variant described herein and from about 99.999% toabout 90.0% by weight composition of one or more adjunct material. Inanother embodiment, the cleaning composition comprises from about0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about2%, or about 0.005% to about 0.5% by weight composition of one or moresubtilisin variant and from about 99.9999% to about 90.0%, about 99.999%to about 98%, about 99.995% to about 99.5% by weight composition of oneor more adjunct material.

In other embodiments, the composition described herein comprises one ormore subtilisin variant described herein and one or more additionalenzyme. The one or more additional enzyme is selected from acyltransferases, alpha-amylases, beta-amylases, alpha-galactosidases,arabinosidases, aryl esterases, beta-galactosidases, carrageenases,catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases,endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases,exo-mannanases, galactanases, glucoamylases, hemicellulases,hyaluronidases, keratinases, laccases, lactases, ligninases, lipases,lipoxygenases, mannanases, metalloproteases, nucleases (e.g. DNases andRNases), oxidases, oxidoreductases, pectate lyases, pectin acetylesterases, pectinases, pentosanases, perhydrolases, peroxidases,phenoloxidases, phosphatases, phospholipases, phytases,polygalacturonases, polyesterases, additional proteases, pullulanases,reductases, rhamnogalacturonases, beta-glucanases, tannases,transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases,xylosidases, and any combination or mixture thereof. Some embodimentsare directed to a combination of enzymes (i.e., a “cocktail”) comprisingconventional enzymes like amylase, lipase, cutinase, mannanase and/orcellulase in conjunction with one or more subtilisin variant describedherein and/or one or more additional protease.

In another embodiment, one or more composition described hereincomprises one or more subtilisin variant described herein and one ormore additional protease. In one embodiment, the additional protease isa serine protease. In another embodiment, the additional protease is analkaline microbial protease or a trypsin-like protease. Suitableadditional proteases include those of animal, plant or microbial origin.In some embodiments, the additional protease is a microbial protease. Inother embodiments, the additional protease is a chemically orgenetically modified mutant. In another embodiment, the additionalprotease is a metalloprotease, a fungal subtilisin, an alkalinemicrobial protease or a trypsin-like protease. Exemplary alkalineproteases include subtilisins derived from, for example, Bacillus (e.g.,subtilis, lentus, amyloliquefaciens, licheniformis, gibsonii, clausii,alkalophilus, subtilisin 309, subtilisin 147 and subtilisin 168).Exemplary additional proteases include but are not limited to thosedescribed in WO92/21760, WO95/23221, WO2008/010925, WO09/149200,WO09/149144, WO09/149145, WO 10/056640, WO10/056653, WO2010/0566356,WO11/072099, WO2011/13022, WO11/140364, WO 12/151534, WO2015/038792,WO2015/089447, WO2015/089441, WO2019180111, US Publ. No. 2008/0090747,U.S. Pat. Nos. 5,801,039, 5,340,735, 5,500,364, 5,855,625, RE 34,606,U.S. Pat. Nos. 5,955,340, 5,700,676 6,312,936, 6,482,628, 8,530,219,U.S. Provisional Appl Nos. 62/180,673 and 62/161,077, and PCT Appl Nos.PCT/US2015/021813, PCT/US2015/055900, PCT/US2015/057497,PCT/US2015/057492, PCT/US2015/057512, PCT/US2015/057526,PCT/US2015/057520, PCT/US2015/057502, PCT/US2016/022282, andPCT/US16/32514, as well as metalloproteases described in WO1999014341,WO1999033960, WO1999014342, WO1999034003, WO2007044993, WO2009058303, WO2009058661, WO2014071410, WO2014194032, WO2014194034, WO 2014194054, andWO 2014/194117. Exemplary additional proteases include, but are notlimited to trypsin (e.g., of porcine or bovine origin) and the Fusariumprotease described in WO89/06270. Exemplary commercial proteasesinclude, but are not limited to MAXATASE®, MAXACAL™, MAXAPEM™,OPTICLEAN®, OPTIMASE®, PROPERASE®, PURAFECT®, PURAFECT® OXP, PURAMAX™,EXCELLASE™ PREFERENZ™ proteases (e.g. P100, P110, P280, P300),EFFECTENZ™ proteases (e.g. P1000, P1050, P2000), EXCELLENZ™ proteases(e.g. P1000), ULTIMASE®, and PURAFAST™ (DuPont); ALCALASE®, BLAZE®, andBLAZE® variants, BLAZE® EVITY® 16L, CORONASE®, SAVINASE®, SAVINASE®ULTRA, SAVINASE® EVITY®, SAVINASE® EVERTS®, PRIMASE®, DURAZYM™,POLARZYME®, OVOZYME®, KANNASE®, LIQUANASE®, LIQUANASE EVERTS®,NEUTRASE®, RELASE® PROGRESS®, EASYZYME®, and ESPERASE® (Novozymes);BLAP™ and BLAP™ variants (Henkel); KAP (B. alkalophilus subtilisin(Kao)); and BIOTOUCH® (AB Enzymes). Exemplary metalloproteases includenprE, the recombinant form of neutral metalloprotease expressed in B.subtilis (See e.g., WO 07/044993), and PMN, the purified neutralmetalloprotease from B. amyloliquefaciens.

Another embodiment is directed to a composition comprising one or moresubtilisin variant described herein and one or more lipase. In someembodiments, the composition comprises from about 0.00001% to about 10%,about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% toabout 2%, or about 0.005% to about 0.5% lipase by weight composition. Anexemplary lipase can be a chemically or genetically modified mutant.Exemplary lipases include, but are not limited to, e.g., those ofbacterial or fungal origin, such as, e.g., H. lanuginosa lipase (see,e.g., EP 258068 and EP 305216), T. lanuginosus lipase (see, e.g., WO2014/059360 and WO2015/010009), Rhizomucor miehei lipase (see, e.g., EP238023), Candida lipase, such as C. antarctica lipase (e.g., C.antarctica lipase A or B) (see, e.g., EP 214761), Pseudomonas lipasessuch as P. alcaligenes and P. pseudoalcaligenes lipase (see, e.g., EP218272), P. cepacia lipase (see, e.g., EP 331376), P. stutzeri lipase(see, e.g., GB 1,372,034), P. fluorescens lipase, Bacillus lipase (e.g.,B. subtilis lipase (Dartois et al., Biochem. Biophys. Acta 1131:253-260(1993)), B. stearothermophilus lipase (see, e.g., JP 64/744992), and B.pumilus lipase (see, e.g., WO 91/16422)). Exemplary cloned lipasesinclude, but not limited to Penicillium camembertii lipase (See,Yamaguchi et al., Gene 103:61-67 (1991)), Geotricum candidum lipase(See, Schimada et al., J. Biochem., 106:383-388 (1989)), and variousRhizopus lipases, such as, R. delemar lipase (See, Hass et al., Gene109:117-113 (1991)), R. niveus lipase (Kugimiya et al., Biosci. Biotech.Biochem. 56:716-719 (1992)) and R. oryzae lipase. Other lipolyticenzymes, such as cutinases, may also find use in one or more compositiondescribed herein, including, but not limited to, e.g., cutinase derivedfrom Pseudomonas mendocina (see, WO 88/09367) and/or Fusarium solanipisi (see, WO90/09446). Exemplary commercial lipases include, but arenot limited to M1 LIPASE™, LUMA FAST™, and LIPOMAX™ (DuPont); LIPEX®,LIPOCLEAN®, LIPOLASE® and LIPOLASE® ULTRA (Novozymes); and LIPASE P™(Amano Pharmaceutical Co. Ltd).

A still further embodiment is directed to a composition comprising oneor more subtilisin variant described herein and one or more amylase. Inone embodiment, the composition comprises from about 0.00001% to about10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001%to about 2%, or about 0.005% to about 0.5% amylase by weightcomposition. Any amylase (e.g., alpha and/or beta) suitable for use inalkaline solutions may be useful to include in such composition. Anexemplary amylase can be a chemically or genetically modified mutant.Exemplary amylases include, but are not limited to those of bacterial orfungal origin, such as, for example, amylases described in GB 1,296,839,WO9100353, WO9402597, WO94183314, WO9510603, WO9526397, WO9535382,WO9605295, WO9623873, WO9623874, WO 9630481, WO9710342, WO9741213,WO9743424, WO9813481, WO 9826078, WO9902702, WO 9909183, WO9919467,WO9923211, WO9929876, WO9942567, WO 9943793, WO9943794, WO 9946399,WO0029560, WO0060058, WO0060059, WO0060060, WO 0114532, WO0134784, WO0164852, WO0166712, WO0188107, WO0196537, WO02092797, WO 0210355,WO0231124, WO 2004055178, WO2004113551, WO2005001064, WO2005003311, WO2005018336, WO2005019443, WO2005066338, WO2006002643, WO2006012899,WO2006012902, WO2006031554, WO 2006063594, WO2006066594, WO2006066596,WO2006136161, WO 2008000825, WO2008088493, WO2008092919, WO2008101894,WO2008/112459, WO2009061380, WO2009061381, WO 2009100102, WO2009140504,WO2009149419, WO 2010/059413, WO 2010088447, WO2010091221, WO2010104675,WO2010115021, WO10115028, WO2010117511, WO 2011076123, WO2011076897,WO2011080352, WO2011080353, WO 2011080354, WO2011082425, WO2011082429,WO 2011087836, WO2011098531, WO2013063460, WO2013184577, WO 2014099523,WO2014164777, and WO2015077126. Exemplary commercial amylases include,but are not limited to AMPLIFY®, DURAMYL®, TERMAMYL®, FUNGAMYL®,STAINZYME®, STAINZYME PLUS®, STAINZYME ULTRA® EVITY®, and BAN™(Novozymes); EFFECTENZ™ S 1000, POWERASE™, PREFERENZ™ S 100, PREFERENZ™S 110, PREFERENZ™ S 210, EXCELLENZ™ S 2000, RAPIDASE® and MAXAMYL® P(DuPont). In some embodiments, the subtilisin variants provided hereinmay be combined with one or more amylases selected from the groupconsisting of AA707, AA560, AAI10, BspAmy24, and CspAmyl, and variantsthereof, and combinations thereof.

Yet a still further embodiment is directed to a composition comprisingone or more subtilisin variant described herein and one or morecellulase. In one embodiment, the composition comprises from about0.00001% to about 10%, 0.0001% to about 10%, about 0.001% to about 5%,about 0.001% to about 2%, or about 0.005% to about 0.5% cellulase byweight of composition. Any suitable cellulase may find use in acomposition described herein. An exemplary cellulase can be a chemicallyor genetically modified mutant. Exemplary cellulases include, but arenot limited to, those of bacterial or fungal origin, such as, forexample, those described in WO2005054475, WO2005056787, U.S. Pat. Nos.7,449,318, 7,833,773, 4,435,307; EP 0495257; and U.S. Provisional Appl.No. 62/296,678. Exemplary commercial cellulases include, but are notlimited to, CELLUCLEAN®, CELLUZYME®, CAREZYME®, ENDOLASE®, RENOZYME®,and CAREZYME® PREMIUM (Novozymes); REVITALENZ™ 100, REVITALENZ™ 200/220,and REVITALENZ® 2000 (DuPont); and KAC-500(B)™ (Kao Corporation). Insome embodiments, cellulases are incorporated as portions or fragmentsof mature wildtype or variant cellulases, wherein a portion of theN-terminus is deleted (see, e.g., U.S. Pat. No. 5,874,276).

An even still further embodiment is directed to a composition comprisingone or more subtilisin variant described herein and one or moremannanase. In one embodiment, the composition comprises from about0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about5%, about 0.001% to about 2%, or about 0.005% to about 0.5% mannanase byweight composition. An exemplary mannanase can be a chemically orgenetically modified mutant. Exemplary mannanases include, but are notlimited to, those of bacterial or fungal origin, such as, for example,those described in WO 2016/007929; U.S. Pat. Nos. 6,566,114; 6,602,842;and 6,440,991: and U.S. Provisional Appl. Nos. 62/251,516, 62/278,383,and 62/278,387. Exemplary commercial mannanases include, but are notlimited to MANNAWAY® (Novozymes) and EFFECTENZ™ M 1000, PREFERENZ® M100, MANNASTAR®, and PURABRITE™ (DuPont).

A yet even still further embodiment is directed to a compositioncomprising one or more subtilisin variant described herein and one ormore peroxidase and/or oxidase enzyme. In one embodiment, thecomposition comprises from about 0.00001% to about 10%, about 0.0001% toabout 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about0.005% to about 0.5% peroxidase or oxidase by weight composition. Aperoxidase may be used in combination with hydrogen peroxide or a sourcethereof (e.g., a percarbonate, perborate or persulfate) and an oxidasemay be used in combination with oxygen. Peroxidases and oxidases areused for “solution bleaching” (i.e., to prevent transfer of a textiledye from a dyed fabric to another fabric when the fabrics are washedtogether in a wash liquor), alone or in combination with an enhancingagent (see, e.g., WO94/12621 and WO95/01426). An exemplary peroxidaseand/or oxidase can be a chemically or genetically modified mutant.Exemplary peroxidases/oxidases include, but are not limited to those ofplant, bacterial, or fungal origin.

Another embodiment is directed to a composition comprising one or moresubtilisin variant described herein, and one or more perhydrolase, suchas, for example, those described in WO2005/056782, WO2007/106293, WO2008/063400, WO2008/106214, and WO2008/106215.

Another embodiment is directed to a composition comprising one or moresubtilisin variant described herein, and one or more pectate lyase, suchas, for example, XPect®.

In yet another embodiment, the one or more subtilisin variant describedherein and one or more additional enzyme contained in one or morecomposition described herein may each independently range to about 10%,wherein the balance of the cleaning composition is one or more adjunctmaterial.

In some embodiments, one or more composition described herein finds useas a detergent additive, wherein said additive is in a solid or liquidform. Such additive products are intended to supplement and/or boost theperformance of conventional detergent compositions and can be added atany stage of the cleaning process. In some embodiments, the density ofthe laundry detergent composition ranges from about 400 to about 1200g/liter, while in other embodiments it ranges from about 500 to about950 g/liter of composition measured at 20° C.

Some embodiments are directed to a laundry detergent compositioncomprising one or more subtilisin variant described herein and one ormore adjunct material selected from surfactants, enzyme stabilizers,builder compounds, polymeric compounds, bleaching agents, additionalenzymes, suds suppressors, dispersants, lime-soap dispersants, soilsuspension agents, anti-redeposition agents, corrosion inhibitors, andcombinations thereof. In some embodiments, the laundry compositions alsocontain softening agents.

Further embodiments are directed to manual dishwashing compositioncomprising one or more subtilisin variant described herein and one ormore adjunct material selected from surfactants, organic polymericcompounds, suds enhancing agents, group II metal ions, solvents,hydrotropes, and additional enzymes.

Other embodiments are directed to one or more composition describedherein, wherein said composition is a compact granular fabric cleaningcomposition that finds use in laundering colored fabrics or providessoftening through the wash capacity, or is a heavy duty liquid (HDL)fabric cleaning composition. Exemplary fabric cleaning compositionsand/or processes for making such compositions are described in USPNs6,610,642 and 6,376,450. Other exemplary cleaning compositions aredescribed, for example, in U.S. Pat. Nos. 6,605,458; 6,294,514;5,929,022; 5,879,584; 5,691,297; 5,565,145; 5,574,005; 5,569,645;5,565,422; 5,516,448; 5,489,392; and 5,486,303; 4,968,451; 4,597,898;4,561,998; 4,550,862; 4,537,706; 4,515,707; and 4,515,705.

In some embodiments, the cleaning compositions comprise an acidifyingparticle or an amino carboxylic builder. Examples of an amino carboxylicbuilder include aminocarboxylic acids, salts and derivatives thereof. Insome embodiment, the amino carboxylic builder is an aminopolycarboxylicbuilder, such as glycine-N,N-diacetic acid or derivative of generalformula MOOC—CHR-N(CH₂COOM)₂ where R is C₁₋₁₂alkyl and M is alkalimetal. In some embodiments, the amino carboxylic builder can bemethylglycine diacetic acid (MGDA), GLDA (glutamic-N,N-diacetic acid),iminodisuccinic acid (IDS), carboxymethyl inulin and salts andderivatives thereof, aspartic acid-N-monoacetic acid (ASMA), asparticacid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid(ASMP), N-(2-sulfomethyl) aspartic acid (SMAS), N-(2-sulfoethyl)asparticacid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), IDA (iminodiacetic acid) and salts and derivativesthereof such as N-methyliminodiacetic acid (MIDA),alpha-alanine-N,N-diacetic acid (alpha-ALDA), serine-N,N-diacetic acid(SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diaceticacid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilicacid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA) andsulfomethyl-N,N-diacetic acid (SMDA) and alkali metal salts andderivative thereof. In some embodiments, the acidifying particle has aweight geometric mean particle size of from about 400 microns to about1200 microns and a bulk density of at least 550 g/L. In someembodiments, the acidifying particle comprises at least about 5% of thebuilder.

In some embodiments, the acidifying particle can comprise any acid,including organic acids and mineral acids. Organic acids can have one ortwo carboxyls and in some instances up to 15 carbons, especially up to10 carbons, such as formic, acetic, propionic, capric, oxalic, succinic,adipic, maleic, fumaric, sebacic, malic, lactic, glycolic, tartaric andglyoxylic acids. In some embodiments, the acid is citric acid. Mineralacids include hydrochloric and sulfuric acid. In some instances, theacidifying particle is a highly active particle comprising a high levelof amino carboxylic builder. Sulfuric acid has also been found tofurther contribute to the stability of the final particle.

Additional embodiments are directed to a cleaning composition comprisingone or more subtilisin variant and one or more surfactant and/orsurfactant system, wherein the surfactant is selected from nonionicsurfactants, anionic surfactants, cationic surfactants, ampholyticsurfactants, zwitterionic surfactants, semi-polar nonionic surfactants,and mixtures thereof. In some embodiments, the surfactant is present ata level of from about 0.1 to about 60%, while in alternative embodimentsthe level is from about 1 to about 50%, while in still furtherembodiments the level is from about 5 to about 40%, by weight of thecleaning composition.

In some embodiments, one or more composition described herein comprisesone or more detergent builders or builder systems. In one embodiment,the composition comprises from about 1% or greater, from about 0.1% toabout 80%, from about 3% to about 60%, from about 5% to about 40%, orfrom about 10% to about 50% builder by weight composition. Exemplarybuilders include, but are not limited to alkali metal; ammonium andalkanolammonium salts of polyphosphates; alkali metal silicates;alkaline earth and alkali metal carbonates; aluminosilicates;polycarboxylate compounds; ether hydroxypolycarboxylates; copolymers ofmaleic anhydride with ethylene or vinyl methyl ether, 1, 3, 5-trihydroxybenzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid;ammonium and substituted ammonium salts of polyacetic acids such asethylenediamine tetraacetic acid and nitrilotriacetic acid;polycarboxylates such as mellitic acid, succinic acid, citric acid,oxydisuccinic acid, polymaleic acid, benzene 1,3,5-tricarboxylic acid,carboxymethyloxysuccinic acid; and soluble salts thereof. In some suchcompositions, the builders form water-soluble hardness ion complexes(e.g., sequestering builders), such as citrates and polyphosphates,e.g., sodium tripolyphosphate, sodium tripolyphospate hexahydrate,potassium tripolyphosphate, and mixed sodium and potassiumtripolyphosphate. Exemplary builders are described in, e.g., EP 2100949.In some embodiments, the builders include phosphate builders andnon-phosphate builders. In some embodiments, the builder is a phosphatebuilder. In some embodiments, the builder is a non-phosphate builder. Insome embodiments, the builder comprises a mixture of phosphate andnon-phosphate builders. Exemplary phosphate builders include, but arenot limited to mono-phosphates, di-phosphates, tri-polyphosphates oroligomeric-polyphosphates, including the alkali metal salts of thesecompounds, including the sodium salts. In some embodiments, a buildercan be sodium tripolyphosphate (STPP). Additionally, the composition cancomprise carbonate and/or citrate. Other suitable non-phosphate buildersinclude homopolymers and copolymers of polycarboxylic acids and theirpartially or completely neutralized salts, monomeric polycarboxylicacids and hydroxycarboxylic acids and their salts. In some embodiments,salts of the above-mentioned compounds include the ammonium and/oralkali metal salts, i.e. the lithium, sodium, and potassium salts,including sodium salts. Suitable polycarboxylic acids include acyclic,alicyclic, hetero-cyclic and aromatic carboxylic acids, wherein in someembodiments, they can contain at least two carboxyl groups which are ineach case separated from one another by, in some instances, no more thantwo carbon atoms.

In some embodiments, one or more composition described herein comprisesone or more chelating agent. In one embodiment, the compositioncomprises from about 0.1% to about 15% or about 3% to about 10%chelating agent by weight composition. Exemplary chelating agentsinclude, but are not limited to, e.g., copper, iron, manganese, andmixtures thereof.

In some embodiments, one or more composition described herein comprisesone or more deposition aid. Exemplary deposition aids include, but arenot limited to, e.g., polyethylene glycol; polypropylene glycol;polycarboxylate; soil release polymers, such as, e.g., polyterephthalicacid; clays such as, e.g., kaolinite, montmorillonite, attapulgite,illite, bentonite, and halloysite; and mixtures thereof.

In other embodiments, one or more composition described herein comprisesone or more anti-redeposition agent or non-ionic surfactant (which canprevent the re-deposition of soils) (see, e.g., EP 2100949). Forexample, in ADW compositions, non-ionic surfactants find use for surfacemodification purposes, in particular for sheeting, to avoid filming andspotting and to improve shine. These non-ionic surfactants also find usein preventing the re-deposition of soils. In some embodiments, thenon-ionic surfactant can be ethoxylated nonionic surfactants,epoxy-capped poly(oxyalkylated) alcohols and amine oxides surfactants.

In some embodiments, one or more composition described herein comprisesone or more dye transfer inhibiting agent. Exemplary polymeric dyetransfer inhibiting agents include, but are not limited to,polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers ofN-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones,polyvinylimidazoles, and mixtures thereof. In one embodiment, thecomposition comprises from about 0.0001% to about 10%, about 0.01% toabout 5%, or about 0.1% to about 3% dye transfer inhibiting agent byweight composition.

In some embodiments, one or more composition described herein comprisesone or more silicate. Exemplary silicates include, but are not limitedto, sodium silicates, e.g., sodium disilicate, sodium metasilicate, andcrystalline phyllosilicates. In some embodiments, silicates are presentat a level of from about 1% to about 20% or about 5% to about 15% byweight of the composition.

In some still additional embodiments, one or more composition describedherein comprises one or more dispersant. Exemplary water-soluble organicmaterials include, but are not limited to, e.g., homo- or co-polymericacids or their salts, in which the polycarboxylic acid comprises atleast two carboxyl radicals separated from each other by not more thantwo carbon atoms.

In some further embodiments, one or more composition described hereincomprises one or more inorganic enzyme stabilizer. In some embodiments,the enzyme stabilizer is water-soluble sources of calcium and/ormagnesium ions. In some embodiments, the enzyme stabilizers includeoligosaccharides, polysaccharides, and inorganic divalent metal salts,including alkaline earth metals, such as calcium salts. In someembodiments, the enzymes employed herein are stabilized by the presenceof water-soluble sources of zinc (II), calcium (II) and/or magnesium(II) ions in the finished compositions that provide such ions to theenzymes, as well as other metal ions (e.g., barium (II), scandium (II),iron (II), manganese (II), aluminum (III), tin (II), cobalt (II), copper(II), nickel (II), and oxovanadium (IV)). Chlorides and sulfates alsofind use in some embodiments. Exemplary oligosaccharides andpolysaccharides (e.g., dextrins) are described, for example, in WO07/145964. In some embodiments, reversible protease inhibitors also finduse, such as boron-containing compounds (e.g., borate, 4-formyl phenylboronic acid, and phenyl-boronic acid derivatives (such for example,those described in WO96/41859) and/or a peptide aldehyde, such as, forexample, is further described in WO2009/118375 and WO2013004636.

Peptidic inhibitors can be naturally derived or synthetically producedoligopeptides able to bind to protease and inhibit its proteolyticactivity, and thus used as protease stabilizers in liquid laundryformulations. Peptide aldehydes are peptidic inhibitors and may be usedas protease stabilizers in detergent formulations as previouslydescribed (WO199813458, WO2011036153, US20140228274). Examples ofpeptide aldehyde stabilizers are peptide aldehydes, ketones, orhalomethyl ketones and might be ‘N-capped’ with for instance a ureido, acarbamate, or a urea moiety, or ‘doubly N-capped’ with for instance acarbonyl, a ureido, an oxiamide, a thioureido, a dithiooxamide, or athiooxamide moiety(EP2358857B1). The molar ratio of these inhibitors tothe protease may be 0.1:1 to 100:1, e.g. 0.5:1-50:1, 1:1-25:1 or2:1-10:1. Other examples of protease stabilizers are benzophenone orbenzoic acid anilide derivatives, which might contain carboxyl groups(U.S. Pat. No. 7,968,508 B2). The molar ratio of these stabilizers toprotease is preferably in the range of 1:1 to 1000:1 in particular 1:1to 500:1 especially preferably from 1:1 to 100:1, most especiallypreferably from 1:1 to 20:1.

In other embodiments, the one or more compositions provided herein doesnot contain an enzyme stabilizer, or peptidic inhibitors, or contains areduced amount of an enzyme stabilizer and peptide inhibitors, such aspeptide aldehydes. That is, the subtilisin variants provided herein havean increased stability with respect to a reference subtilisin incompositions that lack an enzyme stabilizer or peptide inhibitors, orcontain a reduced amount of an enzyme stabilizer or peptide inhibitor.

In some embodiments, one or more composition described herein comprisesone or more bleach, bleach activator, and/or bleach catalyst. In someembodiments, one or more composition described herein comprises one ormore inorganic and/or organic bleaching compound. Exemplary inorganicbleaches include, but are not limited to perhydrate salts, e.g.,perborate, percarbonate, perphosphate, persulfate, and persilicatesalts. In some embodiments, inorganic perhydrate salts are alkali metalsalts. In some embodiments, inorganic perhydrate salts are included asthe crystalline solid, without additional protection, although in someother embodiments, the salt is coated. Bleach activators are typicallyorganic peracid precursors that enhance the bleaching action in thecourse of cleaning at temperatures of 60° C. and below. Exemplary bleachactivators include compounds which, under perhydrolysis conditions, givealiphatic peroxoycarboxylic acids having from about 1 to about 10 carbonatoms or about 2 to about 4 carbon atoms, and/or optionally substitutedperbenzoic acid. Exemplary bleach activators ae described, for example,in EP 2100949. Exemplary bleach catalysts include, but are not limitedto, manganese triazacyclononane and related complexes, as well ascobalt, copper, manganese, and iron complexes. Additional exemplarybleach catalysts are described, for example, in U.S. Pat. Nos.4,246,612; 5,227,084; 4,810,410; WO 99/06521; and EP 2100949.

In some embodiments, one or more composition described herein comprisesone or more catalytic metal complexes. In some embodiments, ametal-containing bleach catalyst finds use. In some embodiments, themetal bleach catalyst comprises a catalyst system comprising atransition metal cation of defined bleach catalytic activity (e.g.,copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganesecations), an auxiliary metal cation having little or no bleach catalyticactivity (e.g., zinc or aluminum cations), and a sequestrate havingdefined stability constants for the catalytic and auxiliary metalcations, particularly ethylenediaminetetraacetic acid,ethylenediaminetetra (methylenephosphonic acid) and water-soluble saltsthereof (see, e.g., U.S. Pat. No. 4,430,243). In some embodiments, oneor more composition described herein is catalyzed by means of amanganese compound. Such compounds and levels of use are described, forexample, in U.S. Pat. No. 5,576,282. In additional embodiments, cobaltbleach catalysts find use and are included in one or more compositiondescribed herein. Various cobalt bleach catalysts are described, forexample, in U.S. Pat. Nos. 5,597,936 and 5,595,967.

In some additional embodiments, one or more composition described hereinincludes a transition metal complex of a macropolycyclic rigid ligand(MRL). As a practical matter, and not by way of limitation, in someembodiments, the compositions and cleaning processes described hereinare adjusted to provide on the order of at least one part per hundredmillion, from about 0.005 ppm to about 25 ppm, about 0.05 ppm to about10 ppm, or about 0.1 ppm to about 5 ppm of active MRL in the washliquor. Exemplary MRLs include, but are not limited to specialultra-rigid ligands that are cross-bridged, such as, e.g.,5,12-diethyl-1,5,8,12-tetraazabicyclo(6.6.2)hexadecane. Exemplary metalMRLs are described, for example, in WO 2000/32601 and U.S. Pat. No.6,225,464.

In another embodiment, one or more composition described hereincomprises one or more metal care agent. In some embodiments, thecomposition comprises from about 0.1% to about 5% metal care agent byweight composition. Exemplary metal care agents include, for example,aluminum, stainless steel, and non-ferrous metals (e.g., silver andcopper). Additional exemplary metal care agents are described, forexample, in EP 2100949, WO 94/26860, and WO 94/26859. In somecompositions, the metal care agent is a zinc salt.

In some embodiments, the cleaning composition is a high density liquid(HDL) composition comprising one or more subtilisin variant describedherein. The HDL liquid laundry detergent can comprise a detersivesurfactant (10-40%) comprising anionic detersive surfactant selectedfrom a group of linear or branched or random chain, substituted orunsubstituted alkyl sulphates, alkyl sulphonates, alkyl alkoxylatedsulphate, alkyl phosphates, alkyl phosphonates, alkyl carboxylates,and/or mixtures thereof; and optionally non-ionic surfactant selectedfrom a group of linear or branched or random chain, substituted orunsubstituted alkyl alkoxylated alcohol, for example, a C₈-C₁₈alkylethoxylated alcohol and/or C₆-C₁₂alkyl phenol alkoxylates, optionallywherein the weight ratio of anionic detersive surfactant (with ahydrophilic index (HIc) of from 6.0 to 9) to non-ionic detersivesurfactant is greater than 1:1. Suitable detersive surfactants alsoinclude cationic detersive surfactants (selected from alkyl pyridiniumcompounds, alkyl quarternary ammonium compounds, alkyl quarternaryphosphonium compounds, alkyl ternary sulphonium compounds, and/ormixtures thereof); zwitterionic and/or amphoteric detersive surfactants(selected from alkanolamine sulpho-betaines); ampholytic surfactants;semi-polar non-ionic surfactants; and mixtures thereof.

In another embodiment, the cleaning composition is a liquid or geldetergent, which is not unit dosed, that may be aqueous, typicallycontaining at least 20% and up to 95% water by weight, such as up toabout 70% water by weight, up to about 65% water by weight, up to about55% water by weight, up to about 45% water by weight, or up to about 35%water by weight. Other types of liquids, including without limitation,alkanols, amines, diols, ethers and polyols may be included in anaqueous liquid or gel. An aqueous liquid or gel detergent may containfrom 0-30% organic solvent. A liquid or gel detergent may benon-aqueous.

The composition can comprise optionally, a surfactancy boosting polymerconsisting of amphiphilic alkoxylated grease cleaning polymers selectedfrom a group of alkoxylated polymers having branched hydrophilic andhydrophobic properties, such as alkoxylated polyalkylen imines in therange of 0.05 wt %-10 wt % and/or random graft polymers typicallycomprising a hydrophilic backbone comprising monomers selected from thegroup consisting of: unsaturated C₁-C₆carboxylic acids, ethers,alcohols, aldehydes, ketones, esters, sugar units, alkoxy units, maleicanhydride, saturated polyalcohols such as glycerol, and mixturesthereof; and hydrophobic side chain(s) selected from the groupconsisting of: C₄-C₂₅alkyl group, polypropylene, polybutylene, vinylester of a saturated C₂-C₆mono-carboxylic acid, C₁-C₆alkyl ester ofacrylic or methacrylic acid, and mixtures thereof.

The composition can comprise additional polymers such as soil releasepolymers including, for example, anionically end-capped polyesters, forexample SRP1; polymers comprising at least one monomer unit selectedfrom saccharide, dicarboxylic acid, polyol and combinations thereof, inrandom or block configuration; ethylene terephthalate-based polymers andco-polymers thereof in random or block configuration, for example,Repel-o-tex SF, SF-2 and SRP6, Texcare SRA100, SRA300, SRN100, SRN170,SRN240, SRN300 and SRN325, Marloquest SL; anti-redeposition polymers(0.1 wt % to 10 wt %, including, for example, carboxylate polymers, suchas polymers comprising at least one monomer selected from acrylic acid,maleic acid (or maleic anhydride), fumaric acid, itaconic acid, aconiticacid, mesaconic acid, citraconic acid, methylenemalonic acid, and anymixture thereof; vinylpyrrolidone homopolymer; and/or polyethyleneglycol with a molecular weight in the range of from 500 to 100,000 Da);cellulosic polymer (including, for example, alkyl cellulose; alkylalkoxyalkyl cellulose; carboxyalkyl cellulose; alkyl carboxyalkylcellulose, examples of which include carboxymethyl cellulose, methylcellulose, methyl hydroxyethyl cellulose, methyl carboxymethylcellulose; and mixtures thereof); and polymeric carboxylate (such as,for example, maleate/acrylate random copolymer or polyacrylatehomopolymer).

The composition can further comprise saturated or unsaturated fattyacid, preferably saturated or unsaturated C₁₂-C₂₄fatty acid (0-10 wt %);deposition aids (including, for example, polysaccharides, cellulosicpolymers, polydiallyl dimethyl ammonium halides (DADMAC), andco-polymers of DADMAC with vinyl pyrrolidone, acrylamides, imidazoles,imidazolinium halides, and mixtures thereof, in random or blockconfiguration; cationic guar gum; cationic cellulose such as cationichydroxyethyl cellulose; cationic starch; cationic polyacylamides; andmixtures thereof.

The composition can further comprise dye transfer inhibiting agentsexamples of which include manganese phthalocyanine, peroxidases,polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers ofN-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones andpolyvinylimidazoles and/or mixtures thereof; chelating agents examplesof which include ethylene-diamine-tetraacetic acid (EDTA); diethylenetriamine penta methylene phosphonic acid (DTPMP); hydroxy-ethanediphosphonic acid (HEDP); ethylenediamine N,N′-disuccinic acid (EDDS);methyl glycine diacetic acid (MGDA); diethylene triamine penta aceticacid (DTPA); propylene diamine tetracetic acid (PDT A);2-hydroxypyridine-N-oxide (HPNO); or methyl glycine diacetic acid(MGDA); glutamic acid N,N-diacetic acid (N,N-dicarboxymethyl glutamicacid tetrasodium salt (GLDA); nitrilotriacetic acid (NTA);4,5-dihydroxy-m-benzenedisulfonic acid; citric acid and any saltsthereof; N-hydroxyethylethylenediaminetri-acetic acid (HEDTA),triethylenetetraaminehexaacetic acid (TTHA), N-hydroxyethyliminodiaceticacid (HEIDA), dihydroxyethylglycine (DHEG),ethylenediaminetetrapropionic acid (EDTP), and derivatives thereof.

The composition can further comprise silicone or fatty-acid based sudssuppressors; an enzyme stabilizer; hueing dyes, calcium and magnesiumcations, visual signaling ingredients, anti-foam (0.001 to about 4.0 wt%), and/or structurant/thickener (0.01-5 wt %) selected from the groupconsisting of diglycerides, triglycerides, ethylene glycol distearate,microcrystalline cellulose, cellulose based materials, microfibercellulose, biopolymers, xanthan gum, gellan gum, and mixtures thereof.

In some embodiments, the cleaning composition is a high density powder(HDD) composition comprising one or more subtilisin variant describedherein. The HDD powder laundry detergent can comprise a detersivesurfactant including anionic detersive surfactants (selected from linearor branched or random chain, substituted or unsubstituted alkylsulphates, alkyl sulphonates, alkyl alkoxylated sulphate, alkylphosphates, alkyl phosphonates, alkyl carboxylates and/or mixturesthereof), non-ionic detersive surfactant (selected from 1 linear orbranched or random chain, substituted or unsubstituted C₈-C₁₈ alkylethoxylates, and/or C₆-C₁₂ alkyl phenol alkoxylates), cationic detersivesurfactants (selected from alkyl pyridinium compounds, alkyl quaternaryammonium compounds, alkyl quaternary phosphonium compounds, alkylternary sulphonium compounds, and mixtures thereof); zwitterionic and/oramphoteric detersive surfactants (selected from alkanolaminesulpho-betaines); ampholytic surfactants; semi-polar non-ionicsurfactants and mixtures thereof; builders (phosphate free builders,e,g., zeolite builders examples of which include zeolite A, zeolite X,zeolite P and zeolite MAP in the range of 0 to less than 10 wt %);phosphate builders, e.g., sodium tri-polyphosphate in the range of 0 toless than 10 wt %; citric acid, citrate salts and nitrilotriacetic acidor salt thereof in the range of less than 15 wt %; silicate salt (sodiumor potassium silicate or sodium meta-silicate in the range of 0 to lessthan 10 wt % or layered silicate (SKS-6)); carbonate salt (sodiumcarbonate and/or sodium bicarbonate in the range of 0 to less than 10 wt%); and bleaching agents (photobleaches, e.g., sulfonated zincphthalocyanines, sulfonated aluminum phthalocyanines, xanthenes dyes,and mixtures thereof); hydrophobic or hydrophilic bleach activators(e.g., dodecanoyl oxybenzene sulfonate, decanoyl oxybenzene sulfonate,decanoyl oxybenzoic acid or salts thereof, 3,5,5-trimethy hexanoyloxybenzene sulfonate, tetraacetyl ethylene diamine-TAED, andnonanoyloxybenzene sulfonate-NOBS, nitrile quats, and mixtures thereof);hydrogen peroxide; sources of hydrogen peroxide (inorganic perhydratesalts, e.g., mono or tetra hydrate sodium salt of perborate,percarbonate, persulfate, perphosphate, or persilicate); preformedhydrophilic and/or hydrophobic peracids (selected from percarboxylicacids and salts, percarbonic acids and salts, perimidic acids and salts,peroxymonosulfuric acids and salts, and mixtures thereof); and/or bleachcatalyst (e.g., imine bleach boosters, such as iminium cations andpolyions; iminium zwitterions; modified amines; modified amine oxides;N-sulphonyl imines; N-phosphonyl imines; N-acyl imines; thiadiazoledioxides; perfluoroimines; cyclic sugar ketones and mixtures thereof),metal-containing bleach catalyst (e.g., copper, iron, titanium,ruthenium, tungsten, molybdenum, or manganese cations along with anauxiliary metal cations such as zinc or aluminum and a sequestrate suchas ethylenediaminetetraacetic acid,ethylenediaminetetra(methylenephosphonic acid) and water-soluble saltsthereof).

The composition can further comprise additional detergent ingredientsincluding perfume microcapsules, starch encapsulated perfume accord, anenzyme stabilizer, hueing agents, additional polymers including fabricintegrity and cationic polymers, dye lock ingredients, fabric-softeningagents, brighteners (for example C.I. Fluorescent brighteners),flocculating agents, chelating agents, alkoxylated polyamines, fabricdeposition aids, and/or cyclodextrin.

In some embodiments, the cleaning composition is an automatic (auto)dish washing (ADW) detergent composition comprising one or moresubtilisin variant described herein. The ADW detergent composition cancomprise two or more non-ionic surfactants selected from ethoxylatednon-ionic surfactants, alcohol alkoxylated surfactants, epoxy-cappedpoly(oxyalkylated) alcohols, and amine oxide surfactants present inamounts from 0-10% by wt; builders in the range of 5-60% by wt.comprising either phosphate (mono-phosphates, di-phosphates,tri-polyphosphates or oligomeric-polyphosphates), sodiumtripolyphosphate-STPP or phosphate-free builders (amino acid basedcompounds, e.g., MGDA (methyl-glycine-diacetic acid) and salts andderivatives thereof, GLDA (glutamic-N,Ndiacetic acid) and salts andderivatives thereof, IDS (iminodisuccinic acid) and salts andderivatives thereof, carboxy methyl inulin and salts and derivativesthereof and mixtures thereof, nitrilotriacetic acid (NTA), diethylenetriamine penta acetic acid (DTPA), and B-alaninediacetic acid (B-ADA)and their salts), homopolymers and copolymers of poly-carboxylic acidsand their partially or completely neutralized salts, monomericpolycarboxylic acids and hydroxycarboxylic acids and their salts in therange of 0.5-50% by wt; sulfonated/carboxylated polymers (providedimensional stability to the product) in the range of about 0.1 to about50% by wt; drying aids in the range of about 0.1 to about 10% by wt(selected from polyesters, especially anionic polyesters optionallytogether with further monomers with 3-6 functionalities which areconducive to polycondensation, specifically acid, alcohol or esterfunctionalities, polycarbonate-, polyurethane- and/orpolyurea-polyorganosiloxane compounds or precursor compounds thereof ofthe reactive cyclic carbonate and urea type); silicates in the rangefrom about 1 to about 20% by wt (sodium or potassium silicates, e.g.,sodium disilicate, sodium meta-silicate and crystallinephyllosilicates); bleach-inorganic (e.g., perhydrate salts such asperborate, percarbonate, perphosphate, persulfate and persilicate salts)and organic (e.g., organic peroxyacids including diacyl andtetraacylperoxides, especially diperoxydodecanedioic acid,diperoxytetradecanedioic acid, and diperoxyhexadecanedioic acid); bleachactivator-organic peracid precursors in the range from about 0.1 toabout 10% by wt; bleach catalysts (selected from manganesetriazacyclononane and related complexes, Co, Cu, Mn and Febispyridylamine and related complexes, and pentamine acetate cobalt(III)and related complexes); metal care agents in the range from about 0.1-5%by wt (selected from benzatriazoles, metal salts and complexes, andsilicates); enzymes in the range from about 0.01-5.0 mg of active enzymeper gram of ADW detergent composition (acyl transferases,alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases,aryl esterases, beta-galactosidases, carrageenases, catalases,cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1,4-glucanases, endo-beta-mannanases, esterases, exo-mannanases,galactanases, glucoamylases, hemicellulases, hyaluronidases,keratinases, laccases, lactases, ligninases, lipases, lipoxygenases,mannanases, oxidases, oxidoreductases, pectate lyases, pectin acetylesterases, pectinases, pentosanases, peroxidases, phenoloxidases,phosphatases, phospholipases, phytases, polyestersases,polygalacturonases, proteases, pullulanases, reductases,rhamnogalacturonases, beta-glucanases, tannases, transglutaminases,xylan acetyl-esterases, xylanases, xyloglucanases, xylosidases, andmixtures thereof); and enzyme stabilizer components (selected fromoligosaccharides, polysaccharides and inorganic divalent metal salts).

More embodiments are directed to compositions and methods of treatingfabrics (e.g., to desize a textile) using one or more subtilisin variantdescribed herein. Fabric-treating methods are well known in the art(see, e.g., U.S. Pat. No. 6,077,316). For example, the feel andappearance of a fabric can be improved by a method comprising contactingthe fabric with a variant described herein in a solution. The fabric canbe treated with the solution under pressure.

One or more subtilisin variant described herein can be applied during orafter weaving a textile, during the desizing stage, or one or moreadditional fabric processing steps. During the weaving of textiles, thethreads are exposed to considerable mechanical strain. Prior to weavingon mechanical looms, warp yarns are often coated with sizing starch orstarch derivatives to increase their tensile strength and to preventbreaking. One or more subtilisin variant described herein can be usedalone or with other desizing chemical reagents and/or desizing enzymesto desize fabrics, including cotton-containing fabrics, as detergentadditives, e.g., in aqueous compositions. An amylase also can be used incompositions and methods for producing a stonewashed look on indigo-dyeddenim fabric and garments. For the manufacture of clothes, the fabriccan be cut and sewn into clothes or garments, which are afterwardsfinished. In particular, for the manufacture of denim jeans, differentenzymatic finishing methods have been developed. The finishing of denimgarment normally is initiated with an enzymatic desizing step, duringwhich garments are subjected to the action of proteolytic enzymes toprovide softness to the fabric and make the cotton more accessible tothe subsequent enzymatic finishing steps. One or more subtilisin variantdescribed herein can be used in methods of finishing denim garments(e.g., a “bio-stoning process”), enzymatic desizing and providingsoftness to fabrics, and/or finishing process.

One or more subtilisin variant described herein finds further use in theenzyme aided bleaching of paper pulps such as chemical pulps,semi-chemical pulps, kraft pulps, mechanical pulps or pulps prepared bythe sulfite method. In general terms, paper pulps are incubated with oneor more subtilisin variant described herein under conditions suitablefor bleaching the paper pulp.

In some embodiments, the pulps are chlorine free pulps bleached withoxygen, ozone, peroxide or peroxyacids. In some embodiments, one or moresubtilisin variant described herein is used in enzyme aided bleaching ofpulps produced by modified or continuous pulping methods that exhibitlow lignin contents. In some other embodiments, one or more subtilisinvariant described herein is applied alone or preferably in combinationwith xylanase and/or endoglucanase and/or alpha-galactosidase and/orcellobiohydrolase enzymes.

The following examples are provided to demonstrate and illustratecertain preferred embodiments and aspects of the present disclosure andshould not be construed as limiting.

Example 1 Construction and Expression of Subtilisin Protease Variants

Variants of a series of subtilisins of bacterial origin having one, twoor more substitutions in each of the parental backbones (Table 1) weregenerated using molecular biology techniques known in the art. Librariesof genes were generated that have various combinations of the followingamino acid features: X003T, X003V, X009E, X024Q, X040E, X069S, X076D,X078N, X079I, X087D, X118R, X124I, X128R, X128S, X129P, X130S, X145R,X166Q, X182E, X185Q, X210I, X211P, X217L, X218S, X248D, X259P, listed inBPN′ (SEQ ID NO:1) numbering. Libraries of constructs for eachsubtilisin protease (parent and variants) were transformed into asuitable Bacillus subtilis strain using methods known in the art. Thetransformation mixtures were plated on LA containing skim milk and theappropriate antibiotic resistance selection. Single colonies were pickedand grown on Luria broth with the appropriate antibiotic resistanceselection. The DNA was extracted and the sequence of each gene ofinterest was confirmed by PacBio sequencing method.

For recombinant protein expression experiments, transformed cells weregrown in 96-well microtiter plates (MTPs) in cultivation medium(enriched semi-defined media based on MOPs buffer, with urea as majornitrogen source, glucose as the main carbon source, supplemented with 1%soytone for robust cell growth, containing antibiotic selection) for 3days at 32° C., 300 rpm, with 80% humidity in shaking incubator. Aftercentrifugation and filtration, clarified culture supernatants containingthe proteases of interest were used for assays.

Table 1 below provides the names and sequences for the subtilisinparental backbones (parent) used in this study. All subtilisins, withthe exception of DSM14391 and CP474, were cloned and expressed usingtheir own (wildtype) propeptide sequences. For expression of DSM14391and CP474, the B. lentus subtilisin propeptide (SEQ ID NO: 40) was usedinstead, but the naturally occurring propeptide sequences for theseprotease are listed on Table 1. Prior references and accession numbersfor the various subtilisin parent backbones of this study are providedon Table 1. The DNA sequence encoding the expression cassette for thepro-mature polypeptide for each parental backbone is listed on Table 1,along with the pro-peptide and predicted mature protein sequences foreach protease.

TABLE 1 List of subtilisin backbones used for evaluation of variantswith improved stability. Prior patent references and sequence ID NOs, oraccession numbers are provided. SEQ ID Nos pro- mature peptide proteinPrior patent references or DNA AA AA Subtilisin accession numbersequence sequence sequence AprE (subtilisin E) WP_003233171 24 41 8WP_082194748 WP_082194748 [formerly listed as 25 42 9 WP_008359041]Chemgen_164A SEQ ID NO: 2 in U.S. Pat. No. 26 43 10 5,275,945 CP474 Avariant of LG12 SprC protease 27 40 11 (SprC is SEQ ID NO: 3 inWO2015/038792) ZP-00454 A variant of WP_010192403 28 44 12 (previouslyZP_07707657) (ZP_07707657 is SEQ ID NO: 7 in WO2015/038792) Bpan01744SEQ ID NO: 3 in WO2016069563 29 45 13 DSM14391 SEQ ID NO: 13 inWO2018/118917 30 46 14 BspAK01305 SEQ ID NO: 6 in WO2016/069569 31 47 15BspAI02518 SEQ ID NO: 3 in WO2015/089441 32 48 16 BspZ00056 SEQ ID NO: 9in WO 2016/069544 33 49 17 Bad02409 SEQ ID NO: 13 in WO2010/69557 34 2318 Bba02069 SEQ ID NO: 3 in WO2016/061438 35 39 19 BspZ00258 SEQ ID NO:9 in WO 2016/069552 38 36 22

Example 2 Enzyme Assays

Protein Determination Assay: Culture supernatants were diluted into 10mM NaCl, 0.1 mM CaCl₂), 0.005% Tween® 80 to a concentration that fitswithin the linear range of the standard curve for loading onto column.For high resolution concentration determinations, high performanceliquid chromatography (HPLC) method was performed on protein samples. AnAgilent 1100 HPLC equipped with an Agilent 300SB-C8 column was used forprotein quantitation. Samples were eluted from the column using agradient of 0.1% trifluoroacetic acid (TFA) in water and 0.1% TFA inacetonitrile. Absorbance was measured at 220 nm, and peaks wereintegrated using ChemStation software (Agilent Technologies, USA). Theprotein concentrations of the samples were calculated based on astandard curve of a purified protease.

Alternatively, the concentration of the sample proteases in culturesupernatant was determined by UHPLC using a Zorbax 300 SB-C3 column andlinear gradient of 0.1% Trifluoroacetic acid (Buffer A) and 0.07%Trifluoroacetic acid in Acetonitrile (Buffer B) with absorbancedetection at 220 nm. The protein concentration of the samples wascalculated using a standard curve of the purified protease.

Protease Activity: The protease activity of parent and variants thereofwas tested by measuring the hydrolysis of N-suc-AAPF-pNA substrate. Forthe AAPF assay, the reagent solutions used were: 100 mM Tris pH 8.6, 10mM CalCl₂, 0.005% Tween®-80 (Tris/Ca buffer) and 160 mM suc-AAPF-pNA inDMSO (suc-AAPF-pNA stock solution) (Sigma: S-7388). To prepare a workingsolution, 1 mL suc-AAPF-pNA stock solution was added to 100 mL Tris/Cabuffer and mixed. An enzyme sample was added to a microtiter plate (MTP)containing 1 mg/mL suc-AAPF-pNA working solution and assayed foractivity at 405 nm over 3-5 min using a SpectraMax plate reader inkinetic mode at room temperature (RT). The protease activity wasexpressed as mOD/min.

Cleaning performance assays: Detergents used in these studies include:Persil Small & Mighty Non-Bio Liquid Detergent “Persil Non-Bio” (PNB,Unilever) heavy duty liquid laundry (HDL) purchased in 2014 from localsupermarket; GSM-B Phosphate-free automatic dishwashing (ADW) formulapurchased without enzymes from WFK Testgewebe GmbH, Brüggen, Deutschland(www.testgewebe.de), composition listed on Table 2; and ECE2 heavy dutypowder detergent (HDD) from WFK Testgewebe GmbH, Brüggen, Deutschland(www.testgewebe.de), composition listed on Table 3. Table 4 lists theconditions used for the cleaning performance assays. Persil Non-BioSmall & Mighty (Persil Non-Bio, PNB), is considered boron-free since itcontains≤5 mg/Kg of boron, when tested for elemental boron content.

TABLE 2 Composition of GSM-B Phosphate- Free Detergent (GSM-B, pH 10.5)Component wt % Sodium citrate dehydrate 30 Maleic acid/acrylic acidcopolymer sodium Salt 12 (SOKALAN ® CP5, BASF) Sodium perboratemonohydrate 5 TAED 2 Sodium disilicate: Protil A (Cognis) 25 Linearfatty alcohol ethoxylate 2 Sodium carbonate anhydrous add to 100

TABLE 3 Composition of ECE-2 powder detergent (HDD) Weight Component %Linear sodium alkyl benzene sulfonate 9.7 Ethoxylated fatty alcoholC12-18 (7 EO) 5.2 Sodium soap 3.6 Antifoam DC2-4248S 4.5 Sodium aluminumsilicate zeolite 4A 32.5 Sodium carbonate 11.8 Sodium salt of acopolymer from acrylic and maleic acid 5.2 (Sokalan CP5) Sodium silicate(SiO2:Na2O = 3.3:1) 3.4 Carboxymethylcellulose 1.3 Diethylene triaminepenta (methylene phosphonic acid) 0.8 Sodium sulfate 9.8 Water 12.2

TABLE 4 Conditions for subtilisin cleaning performance evaluationsHardness Final Wash Conc. Detergent Type Conc, (g/L) (ppm) Buffer pHPersil Non-Bio HDL 2.7 250 5 mM 8.2 (PNB) HEPES GSM-B ADW 3.0 374 notbuffered 10.5 ECE-2 HDD 6.5 374 not buffered 10

Subtilisin variants were tested for cleaning performance relative toeach parent backbone on BMI (EMPA-116, blood/milk/ink on cotton) forlaundry-based HDL and HDD applications, and on egg yolk (PAS-38, eggyolk on polyacryl fabric, aged and colored with carbon black dye) fordish-based applications in 96 well (MTP) microtiter plates. PAS-38swatches and pre-rinsed EMPA116 were purchased from Center forTestmaterials B.V., Vlaardingen. For all stains, pre-punched swatches inMTP plates (Costar 9017 or Greiner 655101) were prepared. Thesemicroswatch-containing plates were filled with detergent solution(listed on Table 4) prior to enzyme addition. Aliquots of enzyme wereadded to detergent-filled MTPs containing microswatches to reach a finalvolume of 180 microliters for laundry and ADW assays. Laundry cleaningassays with HDL and HDD formulas were carried out at 25° C. for 20 min,while ADW assays were carried out at 40° C. for 30 min. Followingincubation, 100-150 microliters of supernatant was transferred to afresh MTP and absorbance was read at 405 nm using a SpectraMax platereader. Absorbance results were obtained by subtracting the value for ablank control (no enzyme) from each sample value. For each condition andsubtilisin variant in Example 3, a cleaning performance index (PI) wascalculated by dividing the blank subtracted absorbance of the variant bythat of the respective parent protease at the same concentration. Theblank subtracted absorbance value for the parent protease at thecorresponding concentration of the variant was determined using astandard curve of the parent protease, which was included in the testand was generated using a Langmuir fit or Hill Sigmoidal fit, asappropriate. Results for each subtilisin variant sample were compared tothe results for the parent molecule in each assay plate to generate anormalized PI and mitigate plate to plate variation.

Detergent Stability Assay: Subtilisin enzymes were tested for stabilityin 10% PNB detergent (10-fold dilution of commercial detergent) attemperatures specified on Table 5 to determine the residual activityfollowing incubation at elevated temperature. The elevated temperaturewas set to enable discrimination of residual activity of the stressedsample compared to the unstressed sample during an incubation period of20 minutes in a range appropriate to discern differences of variantenzymes versus their parent. A diluted enzyme sample was mixed inappropriate detergent and the protease activity on AAPF substrate wasmeasured immediately, to serve as the unstressed value. The samples weresubsequently placed in a PCR plate, sealed and incubated at elevatedtemperature for 20 min using a thermocycler, then assayed for AAPFactivity to obtain the stressed value. Assays were carried out in 384well MTPs. The residual activity was calculated by dividing the stressedactivity by the unstressed activity for each enzyme. In some instances,the relative stability of the variant enzymes is reported at aperformance index (PI), and in other instances it is reported at apercent residual activity (% RA). The stability Performance Index (PI)for each variant under each assay condition was obtained by dividing theresidual activity of the variant by the residual activity of the parentwild type. The percent residual activity for each variant under eachassay condition was obtained by dividing the AAPF activity absorbancefor stressed sample by the AAPF activity absorbance for unstressedsample and multiplying by 100.

TABLE 5 Stress Conditions for Stability Tests in 10% PNB detergent 20min incubation at Subtilisin Backbone Temperature (° C.) AprE 41-42WP_082194748 46 Chemgen_164A 51-56 CP474 37 ZP-00454 42 Bpan01744 44-46DSM14391 30-36 BspAI02518 30-36 BspZ00056 63-64 Bad02409 67 Bba0206939-40 BspAK01305 47 BspZ00258 62

Example 3 AprE & WP_082194748 Subtilisin Variants with ImprovedStability in Detergent

Variants of AprE (Subtilisin E, SEQ ID NO: 8) and WP_082194748 (SEQ IDNO: 9) subtilisins were evaluated for stability and cleaning performanceusing methods described in Example 2, and performance index for eachvariant was calculated versus the respective parent molecule. The AprE(Subtilisin E) and WP_082194748 subtilisin are more closely related insequence to BPN′ subtilisin than to other known subtilisins (86.5% and76.4% amino acid sequence identity, respectively).

Detergent stability results are reported as either performance index(PI) or % residual activity (% RA). Tables 6A and 6B show the stabilityresults for AprE (Subtilisin E), and Table 8 for WP_082194748 variantshaving stability PI values 1.1 and greater, where the cleaningperformance index was at least 0.5 or greater (relative to parent) in atleast one cleaning assay. Tables 7 and 9 show the cleaning assaysresults for AprE variants in Table 6A and WP_082194748 variants in Table8 respectively, having cleaning performance PI values 1.0 or greater forat least one condition when compared to the respective parentsubtilisin, and also displaying stability PI values 1.1 or greater.

TABLE 6A AprE subtilisin variants with improved stability in liquiddetergent at 41° C. (PI values ≥ 1.1) compared to AprE parent AprEVariant Substitutions in Substitutions in Stability Sample ID AprEnumbering BPN′ numbering PI AprE-00772 S003V S003V 1.8 AprE-00795 N076DN076D 2.0 AprE-00488 S078N S078N 1.6 AprE-00944 G166Q G166Q 1.9AprE-00511 Y217L Y217L 1.5 AprE-00924 N218S N218S 1.7 AprE-00447 N259PN259P 1.7 AprE-00370 S003V-N259P S003V-N259P 2.0 AprE-00380 S003V-P040ES003V-P040E 1.5 AprE-00413 S003V-M124I S003V-M124I 1.8 AprE-00515S003V-S078N S003V-S078N 1.8 AprE-00729 S003V-N076D S003V-N076D 2.0AprE-00841 S003V-G166Q S003V-G166Q 2.2 AprE-00907 S003V-G128SS003V-G128S 1.8 AprE-00498 A069S-N076D A069S-N076D 1.9 AprE-00594A069S-N218S A069S-N218S 1.6 AprE-00666 A069S-G166Q A069S-G166Q 1.8AprE-00758 A069S-N259P A069S-N259P 1.5 AprE-00788 A069S-S078NA069S-S078N 1.4 AprE-00943 A069S-G128S A069S-G128S 1.4 AprE-00966A069S-M124I A069S-M124I 1.2 AprE-00416 N076D-G128S N076D-G128S 2.5AprE-00774 N076D-S078N N076D-S078N 2.1 AprE-00912 N076D-N218SN076D-N218S 2.3 AprE-00920 N076D-G166Q N076D-G166Q 2.5 AprE-00946N076D-M124I N076D-M124I 2.3 AprE-00365 S078T-M124I S078T-M124I 1.9AprE-00655 S078N-G128S S078N-G128S 2.0 AprE-00891 S078N-N259PS078N-N259P 2.0 AprE-00904 S078N-N218S S078N-N218S 2.0 AprE-00974S078N-G166Q S078N-G166Q 2.1 AprE-00442 M124I-G166Q M124I-G166Q 1.9AprE-00653 M124I-N259P M124I-N259P 1.5 AprE-00770 M124I-G128SM124I-G128S 1.5 AprE-00861 M124I-N218S M124I-N218S 1.7 AprE-00732G128S-N259P G128S-N259P 1.6 AprE-00757 G128S-N218S G128S-N218S 1.7AprE-00824 G128S-G166Q G128S-G166Q 2.0 AprE-00694 G166Q-N259PG166Q-N259P 2.0 AprE-00698 G166Q-N218S G166Q-N218S 2.1 AprE-00646N218S-N259P N218S-N259P 2.0

TABLE 6B Additional AprE subtilisin variants with improved stability inliquid detergent at 42° C., reported as percent residual activity (% RA)compared to AprE parent AprE Variant Substitutions in Substitutions inSample ID AprE numbering BPN′ numbering % RA AprE — — 27 AprE-01081S009E S009E 80 AprE-01080 P040E P040E 100 AprE-01089 S003V-S009ES003V-S009E 88 AprE-01078 S003V-A069S S003V-A069S 42 AprE-01842S003V-N218S S003V-N218S 58 AprE-01082 S009E-P040E S009E-P040E 82AprE-01083 S009E-A069S S009E-A069S 70 AprE-01025 S009E-N076D S009E-N076D96 AprE-01850 S009E-S078N S009E-S078N 75 AprE-01959 S009E-G166QS009E-G166Q 90 AprE-01111 S009E-N218S S009E-N218S 83 AprE-01096S009E-N259P S009E-N259P 84 AprE-01951 P040E-A069S P040E-A069S 33AprE-01108 P040E-N076D P040E-N076D 72 AprE-01844 P040E-S078N P040E-S078N43 AprE-01107 P040E-G166Q P040E-G166Q 75 AprE-01054 P040E-N218SP040E-N218S 65 AprE-01105 P040E-N259P P040E-N259P 48 AprE-01836N076D-N259P N076D-N259P 70

TABLE 7 AprE variants with cleaning performance on par or improvedcompared to AprE parent Cleaning performance, PI AprE Variant BMI stainin PNB PAS-38 stain n GSM- Sample ID detergent B detergent AprE-007721.2 1.2 AprE-00795 1.0 1.1 AprE-00488 1.0 1.1 AprE-00944 1.0 1.1AprE-00511 1.1 1.3 AprE-00924 0.9 1.0 AprE-00447 0.9 1.1 AprE-00370 1.01.0 AprE-00380 1.0 1.0 AprE-00413 1.0 1.0 AprE-00515 1.0 1.2 AprE-007291.0 1.1 AprE-00841 1.1 1.1 AprE-00907 1.0 1.1 AprE-00498 1.0 1.1AprE-00594 1.0 1.1 AprE-00666 0.9 1.1 AprE-00758 1.1 1.1 AprE-00788 1.11.2 AprE-00943 0.9 1.0 AprE-00966 1.0 1.1 AprE-00416 1.1 1.0 AprE-007741.0 1.1 AprE-00912 0.9 1.0 AprE-00920 1.1 1.1 AprE-00946 1.1 1.0AprE-00365 1.0 1.1 AprE-00655 1.1 1.1 AprE-00891 0.9 1.1 AprE-00904 1.01.1 AprE-00974 0.9 1.1 AprE-00442 1.1 1.1 AprE-00653 1.1 1.1 AprE-007701.3 0.9 AprE-00861 1.1 1.1 AprE-00732 1.1 1.0 AprE-00757 1.1 1.0AprE-00824 1.0 1.1 AprE-00694 1.0 1.0 AprE-00698 0.9 1.0 AprE-00646 1.11.1

TABLE 8 WP_082194748 subtilisin variants with improved stability inliquid detergent at 46° C. (PI values > 1.1) compared to WP082194748parent Substitutions in Substitutions WP_082194748 WP_082194748 in BPN′Stability Variant Sample ID numbering numbering PI WP_082194748-00179Y217L Y217L 1.2 WP_082194748-00103 S087D S087D 1.2 WP_082194748-00040T078N T078N 1.4 WP_082194748-00446 G128S G128S 1.4 WP_082194748-00466G166Q G166Q 2.1 WP_082194748-00047 S182E S182E 2.5 WP_082194748-00571G128S-V185Q G128S-V185Q 1.1 WP_082194748-00612 A069S-G128S A069S-G128S1.1 WP_082194748-00380 T078N-V185Q T078N-V185Q 1.3 WP_082194748-00025V185Q-S259P V185Q-S259P 1.5 WP_082194748-00461 G166Q-V185Q G166Q-V185Q1.6 WP_082194748-00441 T078N-S259P T078N-S259P 1.6 WP_082194748-00099T003V-G128S T003V-G128S 1.7 WP_082194748-00306 T078N-G128S T078N-G128S1.7 WP_082194748-00582 G128S-S259P G128S-S259P 1.8 WP_082194748-00486G166Q-S259P G166Q-S259P 1.9 WP_082194748-00242 A069S-M124I A069S-M124I1.9 WP_082194748-00458 T003V-M124I T003V-M124I 1.9 WP_082194748-00546M124I-S259P M124I-S259P 1.9 WP_082194748-00275 M124I-V185Q M124I-V185Q2.0 WP_082194748-00299 T003V-S259P T003V-S259P 2.1 WP_082194748-00066A069S-S259P A069S-S259P 2.1 WP_082194748-00415 M124I-G128S M124I-G128S2.1 WP_082194748-00340 A069S-G166Q A069S-G166Q 2.1 WP_082194748-00038T078N-M124I T078N-M124I 2.2 WP_082194748-00060 M124I-G166Q M124I-G166Q2.5 WP_082194748-00259 T078N-G166Q T078N-G166Q 2.5 WP_082194748-00297T003V-G166Q T003V-G166Q 2.8

TABLE 9 WP_082194748 variants with cleaning performance on par orimproved compared to WP_082194748 parent Cleaning performance, PI BMIstain PAS-38 stain WP_082194748 Variant in PNB in GSM-B Sample IDdetergent detergent WP_082194748-00179 1.0 1.0 WP_082194748-00103 1.11.0 WP_082194748-00040 1.0 1.0 WP_082194748-00446 1.0 0.9WP_082194748-00466 1.0 1.0 WP_082194748-00047 1.1 0.9 WP_082194748-005711.1 0.9 WP_082194748-00612 1.1 0.9 WP_082194748-00380 1.0 1.1WP_082194748-00025 1.0 1.0 WP_082194748-00461 1.0 1.0 WP_082194748-004411.0 1.0 WP_082194748-00099 0.8 1.0 WP_082194748-00306 1.0 1.0WP_082194748-00582 1.1 0.9 WP_082194748-00486 1.1 1.0 WP_082194748-002421.1 0.9 WP_082194748-00458 1.1 1.0 WP_082194748-00546 0.9 1.0WP_082194748-00275 1.2 1.0 WP_082194748-00299 0.8 1.0 WP_082194748-000661.0 1.0 WP_082194748-00340 1.0 1.0 WP_082194748-00038 1.2 1.1WP_082194748-00060 1.0 1.0 WP_082194748-00259 1.0 1.0 WP_082194748-002970.9 1.0

Example 4 Chemgen_164A, CP474, & ZP-00454 Subtilisin Variants withImproved Stability in Detergent

Variants of Chemgen_164A (Chemgen, SEQ ID NO: 10), CP474 (SEQ ID NO: 11)and ZP-00454 (SEQ ID NO: 12) subtilisins were evaluated for stabilityand cleaning performance using methods described in Example 2, andperformance index for each variant was calculated versus the respectiveparent molecule. The Chemgen_164A, CP474, and ZP-00454 subtilisins sharehigh sequence homology with the LG12 (SprC) protease (described inWO2015/038792), having amino acid sequence identities of 81.8%, 79.6%and 90.2%, respectively.

Detergent stability results are reported as either performance index(PI) or residual activity (% RA). Tables 10A and 10B, show the stabilityresults for Chemgen_164A, Table 11 for CP474, and Table 12 for ZP-00454variants having stability PI values 1.1 and greater, where the cleaningperformance index was at least 0.5 or greater (relative to parent) in atleast one cleaning assay. Tables 13, and 14 show the cleaning assayresults for CP474 variants, and ZP-00454 variants respectively, havingcleaning performance PI values 1.0 or greater when compared to therespective parent subtilisin, and also displaying stability PI values1.1 or greater. Due to conditions of the assay, in some instances the PIvalues calculated were very large (due to parent subtilisin activitybeing at level of detection), therefore PI values greater than 4.0 areshown as ≥4.0.

TABLE 10A Chemgen_164A subtilisin variants with improved stability inliquid detergent at 56° C. (PI values ≥ 1.1) compared to Chemgen_164Awildtype (parent) Substitutions in Substitutions Chemgen_164AChemgen_164A in BPN′ Stability variant Sample ID numbering numbering PIChemgen-00272 T003V T003V 3.1 Chemgen-00032 A069S A069S 1.5Chemgen-00626 N087D N087D 3.2 Chemgen-00300 N118R N118R 1.1Chemgen-00173 S129P S129P 1.8 Chemgen-00404 G166Q G166Q 2.2Chemgen-00591 S182E S182E 2.0 Chemgen-00547 N218S N218S 2.4Chemgen-00076 T003V-N076D T003V-N076D 3.1 Chemgen-00108 T003V-N185QT003V-N185Q 3.1 Chemgen-00196 T003V-G128S T003V-G128S 2.9 Chemgen-00329T003V-S129P T003V-S129P 3.2 Chemgen-00378 T003V-G166Q T003V-G166Q 3.2Chemgen-00443 T003V-T078N T003V-T078N 3.2 Chemgen-00481 T003V-A069ST003V-A069S 3.2 Chemgen-00513 T003V-M124I T003V-M124I 2.0 Chemgen-00634T003V-N218S T003V-N218S 3.2 Chemgen-00289 P040E-M124I P040E-M124I 2.5Chemgen-00262 A069S-G128S A069S-G128S 1.2 Chemgen-00394 A069S-G166QA069S-G166Q 2.9 Chemgen-00436 A069S-T078N A069S-T078N 3.2 Chemgen-00444A069S-D259P A069S-D259P 3.0 Chemgen-00525 A069S-S129P A069S-S129P 2.0Chemgen-00527 A069S-N076D A069S-N076D 3.2 Chemgen-00569 A069S-N218SA069S-N218S 2.6 Chemgen-00617 A069S-N185Q A069S-N185Q 1.9 Chemgen-00132N076D-G166Q N076D-G166Q 3.1 Chemgen-00367 N076D-N218S N076D-N218S 3.2Chemgen-00369 N076D-M124I N076D-M124I 3.2 Chemgen-00459 N076D-T078NN076D-T078N 3.2 Chemgen-00546 N076D-D259P N076D-D259P 3.2 Chemgen-00619N076D-S129P N076D-S129P 3.2 Chemgen-00621 N076D-G128S N076D-G128S 3.2Chemgen-00212 T078N-G128S T078N-G128S 2.5 Chemgen-00224 T078N-N185QT078N-N185Q 3.1 Chemgen-00313 T078N-N218S T078N-N218S 3.1 Chemgen-00350T078N-D259P T078N-D259P 3.2 Chemgen-00351 T078N-S129P T078N-S129P 3.2Chemgen-00413 T078N-M124I T078N-M124I 1.5 Chemgen-00560 T078N-G166QT078N-G166Q 3.2 Chemgen-00115 G128S-N218S G128S-N218S 2.1 Chemgen-00448G128S-D259P G128S-D259P 2.2 Chemgen-00517 G128S-N185Q G128S-N185Q 1.1Chemgen-00105 S129P-N185Q S129P-N185Q 1.9 Chemgen-00375 S129P-G166QS129P-G166Q 3.2 Chemgen-00616 S129P-N218S S129P-N218S 2.9 Chemgen-00010G166Q-D259P G166Q-D259P 3.1 Chemgen-00122 G166Q-N185Q G166Q-N185Q 2.9Chemgen-00335 G166Q-N218S G166Q-N218S 3.2 Chemgen-00198 N185Q-N218SN185Q-N218S 2.1 Chemgen-00359 N185Q-D259P N185Q-D259P 2.3 Chemgen-00309N218S-D259P N218S-D259P 3.1

TABLE 10B Chemgen_164A subtilisin variants with improved stability inliquid detergent at 51° C. (reported as percent residual activity, % RA)compared to Chemgen_164A wildtype (parent) Substitutions inSubstitutions Chemgen_164A Chemgen_164A in BPN′ variant Sample IDnumbering numbering % RA Chemgen_164A — — 31 Chemgen-00815 P040E P040E63 Chemgen-00718 N076D N076D 60 Chemgen-00720 T078N T078N 65Chemgen-00723 N185Q N185Q 34 Chemgen-00795 T003V-T009E T003V-T009E 66Chemgen-00794 T003V-P040E T003V-P040E 100 Chemgen-00650 T003V-D259PT003V-D259P 100 Chemgen-00788 T009E-A069S T009E-A069S 36 Chemgen-00712T009E-N076D T009E-N076D 73 Chemgen-00714 T009E-T078N T009E-T078N 57Chemgen-00797 T009E-G166Q T009E-G166Q 58 Chemgen-00798 T009E-N185QT009E-N185Q 36 Chemgen-00741 T009E-D259P T009E-D259P 37 Chemgen-00715P040E-T078N P040E-T078N 84 Chemgen-01467 P040E-G166Q P040E-G166Q 63Chemgen-00716 P040E-N185Q P040E-N185Q 100 Chemgen-01219 P040E-N218SP040E-N218S 49 Chemgen-00804 N076D-N185Q N076D-N185Q 94

TABLE 11 CP474 subtilisin variants with improved stability in liquiddetergent at 37° C. (PI values ≥ 1.1) compared to CP474 parentSubstitutions in Substitutions CP474 Variant CP474 in BPN′ StabilitySample ID numbering numbering PI CP474-00571 T003V T003V 1.8 CP474-00581A040E A040E ≥4.0 CP474-00591 A069S A069S 1.3 CP474-00601 T078N T078N 1.8CP474-00611 T079I T079I ≥4.0 CP474-00631 S162Q S166Q 1.2 CP474-00562N181Q N185Q 1.4 CP474-00563 T003V-S162Q T003V-S166Q 2.5 CP474-00573T003V-N181Q T003V-N185Q 2.1 CP474-00583 T003V-N214S T003V-N218S 1.6CP474-00592 T003V-A040E T003V-A040E ≥4.0 CP474-00593 T003V-D255PT003V-D259P 1.7 CP474-00602 T003V-A069S T003V-A069S 2.3 CP474-00612T003V-T078N T003V-T078N 2.5 CP474-00622 T003V-T079I T003V-T079I ≥4.0CP474-00632 T003V-L124I T003V-L124I 1.5 CP474-00564 A040E-S162QA040E-S166Q ≥4.0 CP474-00574 A040E-N181Q A040E-N185Q ≥4.0 CP474-00584A040E-N214S A040E-N218S ≥4.0 CP474-00594 A040E-D255P A040E-D259P ≥4.0CP474-00603 A040E-A069S A040E-A069S ≥4.0 CP474-00613 A040E-T078NA040E-T078N ≥4.0 CP474-00623 A040E-T079I A040E-T079I ≥4.0 CP474-00633A040E-L124I A040E-L124I ≥4.0 CP474-00565 A069S-N181Q A069S-N185Q 1.4CP474-00604 A069S-T078N A069S-T078N 1.5 CP474-00614 A069S-T079IA069S-T079I ≥4.0 CP474-00634 A069S-S162Q A069S-S166Q 1.5 CP474-00566T078N-D255P T078N-D259P 1.6 CP474-00595 T078N-T079I T078N-T079I ≥4.0CP474-00615 T078N-S162Q T078N-S166Q 2.2 CP474-00625 T078N-N181QT078N-N185Q 2.0 CP474-00635 T078N-N214S T078N-N218S 1.5 CP474-00576T079I-L124I T079I-L124I ≥4.0 CP474-00586 T079I-S162Q T079I-S166Q ≥4.0CP474-00596 T079I-N181Q T079I-N185Q ≥4.0 CP474-00606 T079I-N214ST079I-N218S ≥4.0 CP474-00616 T079I-D255P T079I-D259P ≥4.0 CP474-00597S162Q-N214S S166Q-N218S 1.4 CP474-00579 N181Q-D255P N185Q-D259P 1.4CP474-00617 N181Q-N214S N185Q-N218S 1.3 CP474-00627 N214S-D255PN218S-D259P 1.1

TABLE 12 ZP-00454 subtilisin variants with improved stability in liquiddetergent at 42° C. (PI values ≥ 1.1) compared to ZP-00454 parentSubstitutions in Substitutions ZP-00454 Variant ZP-00454 in BPN′Stability Sample ID numbering numbering PI ZP-00454-00011 A040E A040E2.1 ZP-00454-00021 A069S A069S 1.1 ZP-00454-00031 N076D N076D 1.7ZP-00454-00041 T078N T078N 1.5 ZP-00454-00051 T079I T079I 2.1ZP-00454-00071 I128S I128S 1.2 ZP-00454-00013 A040E-M124I A040E-M124I2.0 ZP-00454-00023 A040E-I128S A040E-I128S 1.7 ZP-00454-00033A040E-S129P A040E-S129P 2.1 ZP-00454-00043 A040E-G166Q A040E-G166Q 2.1ZP-00454-00052 A040E-A069S A040E-A069S 2.2 ZP-00454-00053 A040E-N185QA040E-N185Q 2.3 ZP-00454-00062 A040E-N076D A040E-N076D 2.2ZP-00454-00063 A040E-N218S A040E-N218S 2.1 ZP-00454-00072 A040E-T078NA040E-T078N 2.1 ZP-00454-00073 A040E-D259P A040E-D259P 2.0ZP-00454-00004 A069S-N076D A069S-N076D 1.7 ZP-00454-00005 A069S-N218SA069S-N218S 1.2 ZP-00454-00014 A069S-T078N A069S-T078N 1.7ZP-00454-00024 A069S-T079I A069S-T079I 2.0 ZP-00454-00044 A069S-I128SA069S-I128S 1.2 ZP-00454-00054 A069S-S129P A069S-S129P 1.2ZP-00454-00074 A069S-N185Q A069S-N185Q 1.2 ZP-00454-00006 N076D-N185QN076D-N185Q 1.6 ZP-00454-00016 N076D-N218S N076D-N218S 1.6ZP-00454-00025 N076D-T078N N076D-T078N 1.8 ZP-00454-00026 N076D-D259PN076D-D259P 1.5 ZP-00454-00035 N076D-T079I N076D-T079I 2.1ZP-00454-00045 N076D-M124I N076D-M124I 1.3 ZP-00454-00055 N076D-I128SN076D-I128S 1.8 ZP-00454-00065 N076D-S129P N076D-S129P 1.6ZP-00454-00075 N076D-G166Q N076D-G166Q 1.8 ZP-00454-00007 T078N-N185QT078N-N185Q 1.5 ZP-00454-00027 T078N-D259P T078N-D259P 1.4ZP-00454-00036 T078N-T079I T078N-T079I 2.0 ZP-00454-00056 T078N-I128ST078N-I128S 1.7 ZP-00454-00066 T078N-S129P T078N-S129P 1.5ZP-00454-00076 T078N-G166Q T078N-G166Q 1.6 ZP-00454-00008 T079I-N218ST079I-N218S 2.1 ZP-00454-00018 T079I-D259P T079I-D259P 1.9ZP-00454-00037 T079I-M124I T079I-M124I 2.4 ZP-00454-00047 T079I-I128ST079I-I128S 2.1 ZP-00454-00057 T079I-S129P T079I-S129P 2.0ZP-00454-00067 T079I-G166Q T079I-G166Q 2.0 ZP-00454-00077 T079I-N185QT079I-N185Q 2.0 ZP-00454-00009 I128S-S129P I128S-S129P 1.1ZP-00454-00059 S129P-G166Q S129P-G166Q 1.1

TABLE 13 CP474 variants with cleaning performance on par or improvedcompared to CP474 parent CP474 Variant Cleaning Performance PI, SampleID BMI stain PNB detergent CP474-00591 1.1 CP474-00601 1.0 CP474-006111.1 CP474-00562 1.0 CP474-00573 1.2 CP474-00583 1.1 CP474-00592 1.0CP474-00593 1.1 CP474-00602 1.2 CP474-00612 1.2 CP474-00622 1.2CP474-00574 1.2 CP474-00584 1.1 CP474-00594 1.1 CP474-00603 1.2CP474-00613 1.1 CP474-00623 1.2 CP474-00565 1.2 CP474-00604 1.3CP474-00614 1.4 CP474-00634 1.0 CP474-00595 1.3 CP474-00625 1.2CP474-00635 1.1 CP474-00586 1.2 CP474-00596 1.2 CP474-00606 1.2CP474-00616 1.1 CP474-00597 1.1 CP474-00617 1.3 CP474-00627 1.0

TABLE 14 ZP-00454 variants with cleaning performance on par or improvedcompared to ZP-00454 parent ZP-00454 Variant Cleaning Performance PI,Sample ID BMI stain PNB detergent ZP-00454-00031 1.0 ZP-00454-00041 1.1ZP-00454-00051 2.1 ZP-00454-00033 1.0 ZP-00454-00043 1.0 ZP-00454-000521.1 ZP-00454-00053 1.0 ZP-00454-00024 1.1 ZP-00454-00044 1.0ZP-00454-00054 1.1 ZP-00454-00074 1.0 ZP-00454-00006 1.0 ZP-00454-000161.1 ZP-00454-00025 1.1 ZP-00454-00026 1.0 ZP-00454-00035 1.8ZP-00454-00055 1.0 ZP-00454-00065 1.0 ZP-00454-00075 1.0 ZP-00454-000271.0 ZP-00454-00036 1.0 ZP-00454-00056 1.0 ZP-00454-00076 1.0ZP-00454-00018 1.5 ZP-00454-00037 1.0 ZP-00454-00057 1.7 ZP-00454-000672.2 ZP-00454-00077 1.4 ZP-00454-00059 1.0

Example 5 Bpan01744 Subtilisin Variants with Improved Stability inDetergent

Variants of Bpan01744 (SEQ ID NO: 13) subtilisin were evaluated forstability and cleaning performance using methods described in Example 2,and performance index for each variant was calculated versus the parentmolecule. The Bpan01744 wildtype subtilisin was described as SEQ ID NO:3 in patent application WO2016069563.

Detergent stability results are reported as either performance index(PI) or % residual activity (% RA). Tables 15A and 15B show thestability results for Bpan01744 variants having stability PI values 1.1and greater, where the cleaning performance index was at least 0.5 orgreater (relative to parent) in at least one cleaning assay. Table 16shows the cleaning assays results for Bpan01744 variants from Table 15Ahaving cleaning performance PI values 1.0 or greater for at least onecondition when compared to the parent subtilisin, and also displayingstability PI values 1.1 or greater. Due to conditions of the assay, insome instances the PI values calculated were very large (due to parentsubtilisin activity being at level of detection), therefore PI valuesgreater than 4.0 are shown as ≥4.0.

TABLE 15A Bpan01744 subtilisin variants with improved stability inliquid detergent at 46° C. (PI values ≥ 1.1) compared to Bpan01744parent Substitutions in Substitutions Bpan01744 Bpan01744 in BPN′Stability Variant Sample ID numbering numbering PI Bpan01744-00498 S003VS003V 1.8 Bpan01744-00574 S076N S078N 2.4 Bpan01744-00152 S003V-N179QS003V-N185Q 3.1 Bpan01744-00166 S003V-N074D S003V-N076D ≥4.0Bpan01744-00167 S003V-A067S S003V-A069S 1.9 Bpan01744-00304 S003V-S076NS003V-S078N 3.5 Bpan01744-00417 S003V-N212S S003V-N218S ≥4.0Bpan01744-00544 S003V-N253P S003V-N259P 2.0 Bpan01744-00088 A067S-N074DA069S-N076D ≥4.0 Bpan01744-00153 A067S-G160Q A069S-G166Q 3.8Bpan01744-00414 A067S-N179Q A069S-N185Q 1.7 Bpan01744-00423 A067S-S076NA069S-S078N 2.6 Bpan01744-00488 A067S-N212S A069S-N218S 3.6Bpan01744-00337 N074D-S076N N076D-S078N ≥4.0 Bpan01744-00554 N074D-S127PN076D-S129P ≥4.0 Bpan01744-00158 S076N-G160Q S078N-G166Q ≥4.0Bpan01744-00179 S076N-M122I S078N-M124I 2.1 Bpan01744-00258 S076N-S127PS078N-S129P 3.8 Bpan01744-00121 M122I-N212S M124I-N218S ≥4.0Bpan01744-00362 M122I-S127P M124I-S129P ≥4.0 Bpan01744-00550 M122I-N179QM124I-N185Q 1.6 Bpan01744-00238 S127P-N253P S129P-N259P 1.9Bpan01744-00251 S127P-N179Q S129P-N185Q 2.4 Bpan01744-00282 S127P-N212SS129P-N218S ≥4.0 Bpan01744-00545 S127P-G160Q S129P-G166Q 3.3Bpan01744-00048 G160Q-N253P G166Q-N259P 3.1 Bpan01744-00172 G160Q-N212SG166Q-N218S ≥4.0 Bpan01744-00369 G160Q-N179Q G166Q-N185Q 3.1Bpan01744-00094 N179Q-N212S N185Q-N218S ≥4.0 Bpan01744-00339 N179Q-N253PN185Q-N259P 1.6 Bpan01744-00126 N212S-N253P N218S-N259P 3.5

TABLE 15B Bpan01744 subtilisin variants with improved stability inliquid detergent at 44° C. (reported as percent residual activity, % RA)compared to Bpan01744 parent Substitutions in Substitutions Bpan01744Bpan01744 in BPN′ Variant Sample ID numbering numbering % RA Bpan01744 —— 19 Bpan01744-02141 S009E S009E 36 Bpan01744-01310 N074D N076D 75Bpan01744-00717 N179Q N185Q 23 Bpan01744-00892 N212S N218S 47Bpan01744-01737 N253P N259P 27 Bpan01744-00830 S003V-S009E S003V-S009E58 Bpan01744-01145 S003V-G160Q S003V-G166Q 77 Bpan01744-01257S009E-N074D S009E-N076D 83 Bpan01744-02075 S009E-S076N S009E-S078N 57Bpan01744-01122 S009E-G160Q S009E-G166Q 62 Bpan01744-01123 S009E-N179QS009E-N185Q 33 Bpan01744-00795 S009E-N212S S009E-N218S 69Bpan01744-01124 S009E-N253P S009E-N259P 29 Bpan01744-01035 N074D-G160QN076D-G166Q 74 Bpan01744-01133 N074D-N179Q N076D-N185Q 76Bpan01744-01135 N074D-N212S N076D-N218S 92 Bpan01744-01148 N074D-N253PN076D-N259P 81 Bpan01744-01629 S076N-N179Q S078N-N185Q 37Bpan01744-00991 S076N-N212S S078N-N218S 71 Bpan01744-01151 S076N-N253PS078N-N259P 37

TABLE 16 Bpan01744 variants with cleaning performance on par or improvedcompared to Bpan01744 parent Cleaning Performance PI BMI stain PAS-38stain BMI stain BpaN01744 Variant PNB GSM-B ECE-2 Sample ID detergentdetergent detergent Bpan01744-00498 1.0 1.0 0.9 Bpan01744-00574 0.9 1.11.0 Bpan01744-00166 1.0 0.9 0.9 Bpan01744-00167 1.0 1.0 0.9Bpan01744-00304 1.0 1.0 1.0 Bpan01744-00417 1.0 0.9 0.7 Bpan01744-005440.9 1.1 0.9 Bpan01744-00088 1.0 0.9 0.9 Bpan01744-00414 0.9 1.0 0.9Bpan01744-00423 1.0 0.9 1.0 Bpan01744-00488 0.9 1.0 0.8 Bpan01744-003371.0 1.0 0.9 Bpan01744-00179 1.0 0.9 0.7 Bpan01744-00258 1.0 0.9 0.9Bpan01744-00550 1.0 0.9 0.7 Bpan01744-00238 1.0 0.9 0.9 Bpan01744-002511.0 1.0 0.9 Bpan01744-00339 1.0 1.1 1.0 Bpan01744-00126 0.9 1.0 0.8

Example 6 DSM14391 Subtilisin Variants with Improved Stability inDetergent

Variants of DSM14391 (SEQ ID NO: 14) subtilisin were evaluated forstability using methods described in Example 2, and performance indexfor each variant was calculated versus the parent molecule. The B.gibsonii subtilisin DSM14391 (previously described in SEQ ID NO:13 ofpatent application WO2018118917) shares high sequence homology with B.gibsonii subtilisin Bgi02446 (described previously as SEQ ID NO:11 ofpatent application WO2018118917) with 90% amino acid sequence identity.

Detergent stability results are reported as either performance index(PI) or % residual activity (% RA). Tables 17A and 17B show thestability results for DSM14391 variants having stability PI values 1.1and greater, where the cleaning performance index was at least 0.5 orgreater (relative to parent) in at least one cleaning assay. Due toconditions of the assay, in some instances the PI values calculated werevery large (due to parent subtilisin activity being at level ofdetection), therefore PI values greater than 4.0 are shown as >4.0.

TABLE 17A DSM14391 subtilisin variants with improved stability in liquiddetergent at 36° C. (PI values ≥ 1.1) compared to DSM14391 parentSubstitutions in Substitutions DSM14391 Variant DSM14391 in BPN′Stability Sample ID numbering numbering PI DSM14391-00436 T003V T003V1.2 DSM14391-00091 T009E T009E ≥4.0 DSM14391-00382 S024Q S024Q 1.2DSM14391-00475 S039E S040E ≥4.0 DSM14391-00098 A067S A069S 1.5DSM14391-00189 N074D N076D ≥4.0 DSM14391-00257 S076N S078N 2.6DSM14391-00286 A128S A130S 1.4 DSM14391-00409 G160Q G166Q ≥4.0DSM14391-00289 Q176E Q182E 3.3 DSM14391-00248 R179Q R185Q ≥4.0DSM14391-00202 P212S P218S ≥4.0 DSM14391-00058 N242D N248D 1.2DSM14391-00504 N253P N259P 1.5 DSM14391-00016 T003V-R179Q T003V-R185Q≥4.0 DSM14391-00025 T003V-A067S T003V-A069S 2.2 DSM14391-00028T003V-G160Q T003V-G166Q ≥4.0 DSM14391-00063 T003V-N253P T003V-N259P 2.1DSM14391-00340 T003V-N074D T003V-N076D ≥4.0 DSM14391-00373 T003V-S076NT003V-S078N 3.0 DSM14391-00492 T003V-P212S T003V-P218S ≥4.0DSM14391-00217 S039E-S076N S040E-S078N ≥4.0 DSM14391-00005 A067S-S076NA069S-S078N 3.4 DSM14391-00096 A067S-N253P A069S-N259P 2.5DSM14391-00136 A067S-R179Q A069S-R185Q ≥4.0 DSM14391-00432 A067S-P212SA069S-P218S ≥4.0 DSM14391-00494 A067S-N074D A069S-N076D ≥4.0DSM14391-00007 N074D-S076N N076D-S078N ≥4.0 DSM14391-00168 N074D-P212SN076D-P218S ≥4.0 DSM14391-00230 N074D-D127P N076D-D129P ≥4.0DSM14391-00104 S076N-D127P S078N-D129P 3.0 DSM14391-00113 S076N-N253PS078N-N259P 3.7 DSM14391-00147 S076N-M122I S078N-M124I ≥4.0DSM14391-00252 S076N-P212S S078N-P218S ≥4.0 DSM14391-00302 S076N-R179QS078N-R185Q ≥4.0 DSM14391-00335 M122I-G160Q M124I-G166Q ≥4.0DSM14391-00355 M122I-P212S M124I-P218S ≥4.0 DSM14391-00507 M122I-N253KM124I-N259K ≥4.0 DSM14391-00021 D127P-P212S D129P-P218S ≥4.0DSM14391-00122 D127P-G160Q D129P-G166Q ≥4.0 DSM14391-00367 D127P-R179QD129P-R185Q 1.3 DSM14391-00438 D127P-N253P D129P-N259P 2.3DSM14391-00171 G160Q-R179Q G166Q-R185Q ≥4.0 DSM14391-00430 G160Q-N253PG166Q-N259P ≥4.0 DSM14391-00161 R179Q-P212S R185Q-P218S ≥4.0DSM14391-00203 R179Q-N253P R185Q-N259P ≥4.0

TABLE 17B DSM14391 subtilisin variants with improved stability in liquiddetergent at 30° C. (reported as percent residual activity, % RA)compared to DSM14391 parent Substitutions in Substitutions DSM14391Variant DSM14391 in BPN′ Sample ID numbering numbering % RA DSM14391 — —40 DSM14391-00986 T003V-T009E T003V-T009E 80 DSM14391-00987 T003V-S039ET003V-S040E 74 DSM14391-00863 T009E-S039E T009E-S040E 98 DSM14391-00864T009E-A067S T009E-A069S 86 DSM14391-00839 T009E-N074D T009E-N076D 91DSM14391-00962 T009E-S076N T009E-S078N 84 DSM14391-01005 T009E-R179QT009E-R185Q 94 DSM14391-00971 T009E-P212S T009E-P218S 99 DSM14391-00867T009E-N253P T009E-N259P 76 DSM14391-00968 S039E-A067S S040E-A069S 71DSM14391-00969 S039E-N074D S040E-N076D 83 DSM14391-00985 S039E-R179QS040E-R185Q 96 DSM14391-00977 S039E-P212S S040E-P218S 95 DSM14391-00849S039E-N253P S040E-N259P 72 DSM14391-00974 N074D-R179Q N076D-R185Q 100DSM14391-00976 N074D-N253P N076D-N259P 84 DSM14391-00828 G160Q-P212SG166Q-P218S 96 DSM14391-00844 P212S-N253P P218S-N259P 96

Example 7 BspAI02518 Subtilisin Variants with Improved Stability inDetergent

Variants of BspAI02518 (SEQ ID NO: 16) subtilisin were evaluated forstability and cleaning performance using methods described in Example 2,and performance index for each variant was calculated versus the parentmolecule. The BspAI02518 subtilisin was previously described as SEQ IDNO: 3 in WO2015089441 patent application, and is a member of the B.akibai/clarkii clade of subtilisins.

Detergent stability results are reported as either performance index(PI) or residual activity (% RA). Tables 18A and 18B show the stabilityresults for BspAI02518 variants having stability PI values 1.1 andgreater, where the cleaning performance index was at least 0.5 orgreater (relative to parent) in at least one cleaning assay. Table 19shows the cleaning assays results for BspAI02518 variants from Table 18Ahaving cleaning performance PI values 1.0 or greater for at least onecondition when compared to the parent subtilisin, and also displayingstability PI values 1.1 or greater. Due to conditions of the assay, insome instances the PI values calculated were very large (due to parentsubtilisin activity being at level of detection), therefore PI valuesgreater than 4.0 are shown as ≥4.0.

TABLE 18A BspAI02518 subtilisin variants with improved stability inliquid detergent at 36° C. (PI values ≥ 1.1) compared to BspAI02518parent Substitutions in Substitutions BspAI02518 Variant BspAI02518 inBPN′ Stability Sample ID numbering numbering PI BspAI02518-00709 S003VS003V 2.7 BspAI02518-00637 S009E S009E 2.3 BspAI02518-00689 N074D N076D≥4.0 BspAI02518-00585 S076N S078N 2.8 BspAI02518-00621 M122I M124I 1.3BspAI02518-00941 S176E S182E 2.2 BspAI02518-00764 N179Q N185Q 1.6BspAI02518-00819 N212S N218S 3.5 BspAI02518-00838 N253P N259P 1.3BspAI02518-00506 S003V-N253P S003V-N259P 2.6 BspAI02518-00564S003V-N212S S003V-N218S ≥4.0 BspAI02518-00599 S003V-A067S S003V-A069S1.9 BspAI02518-00624 S003V-N179Q S003V-N185Q 3.3 BspAI02518-00664S003V-G126S S003V-G128S 2.2 BspAI02518-00784 S003V-M122I S003V-M124I 2.7BspAI02518-00897 S003V-N074D S003V-N076D ≥4.0 BspAI02518-00959S003V-S160Q S003V-S166Q ≥4.0 BspAI02518-00405 A067S-N212S A069S-N218S3.1 BspAI02518-00412 A067S-N074D A069S-N076D ≥4.0 BspAI02518-00590A067S-S076N A069S-S078N 2.2 BspAI02518-00646 A067S-N179Q A069S-N185Q 1.3BspAI02518-01025 A067S-S160Q A069S-S166Q 2.7 BspAI02518-00535N074D-N212S N076D-N218S ≥4.0 BspAI02518-00695 N074D-N253P N076D-N259P≥4.0 BspAI02518-00732 N074D-G126S N076D-G128S ≥4.0 BspAI02518-00772N074D-M122I N076D-M124I ≥4.0 BspAI02518-00802 N074D-N179Q N076D-N185Q≥4.0 BspAI02518-00814 N074D-S076N N076D-S078N ≥4.0 BspAI02518-00625S076N-M122I S078N-M124I 2.8 BspAI02518-00800 S076N-N212S S078N-N218S≥4.0 BspAI02518-00937 S076N-N253P S078N-N259P 2.6 BspAI02518-01001S076N-G126S S078N-G128S 2.7 BspAI02518-01032 S076N-N179Q S078N-N185Q 3.4BspAI02518-00594 M122I-G126S M124I-G128S 1.9 BspAI02518-00749M122I-S160Q M124I-S166Q 3.1 BspAI02518-00758 M122I-N179Q M124I-N185Q 1.5BspAI02518-01002 S160Q-N212S S166Q-N218S ≥4.0 BspAI02518-01006S160Q-N253P S166Q-N259P 3.3 BspAI02518-00439 N179Q-N253P N185Q-N259P 1.7BspAI02518-00548 N212S-N253P N218S-N259P 4.0

TABLE 18B BspAI02518 subtilisin variants with improved stability inliquid detergent at 30° C. (reported as percent residual activity, % RA)compared to BspAI02518 parent Substitutions in Substitutions BspAI02518Variant BspAI02518 in BPN′ Sample ID numbering numbering % RA BspAI02518— — 32 BspAI02518-01177 S160Q S166Q 59 BspAI02518-01175 S003V-S009ES003V-S009E 70 BspAI02518-01179 S003V-S076N S003V-S078N 62BspAI02518-01676 S009E-A067S S009E-A069S 45 BspAI02518-01178 S009E-N074DS009E-N076D 82 BspAI02518-01186 S009E-S076N S009E-S078N 68BspAI02518-01991 S009E-S160Q S009E-S166Q 78 BspAI02518-01187 S009E-N179QS009E-N185Q 60 BspAI02518-01811 S009E-N212S S009E-N218S 84BspAI02518-02004 S009E-N253P S009E-N259P 56 BspAI02518-01920 A067S-N253PA069S-N259P 34 BspAI02518-01184 N074D-S160Q N076D-S166Q 86BspAI02518-01190 S076N-S160Q S078N-S166Q 67 BspAI02518-02195 S160Q-N179QS166Q-N185Q 64 BspAI02518-01094 N179Q-N212S N185Q-N218S 73

TABLE 19 BspAI02518 variants with cleaning performance on par orimproved compared to BspAI02518 parent Cleaning performance PIs BMIstain PAS-38 stain BMI stain BspAI02518 Variant in PNB in GSM-B in ECE-2Sample ID detergent detergent detergent BspAI02518-00709 1.1 1.0 1.0BspAI02518-00637 1.4 2.5 1.4 BspAI02518-00689 1.0 1.0 0.8BspAI02518-00585 1.1 1.2 1.1 BspAI02518-00621 1.0 1.2 1.1BspAI02518-00941 0.9 1.0 0.8 BspAI02518-00764 0.9 1.2 1.1BspAI02518-00819 1.0 1.0 0.9 BspAI02518-00838 1.1 1.0 1.0BspAI02518-00506 1.0 1.0 0.8 BspAI02518-00564 1.0 0.9 1.0BspAI02518-00599 1.4 2.4 1.3 BspAI02518-00624 1.1 1.6 1.1BspAI02518-00664 1.1 1.0 0.9 BspAI02518-00784 1.0 1.0 0.9BspAI02518-00897 1.1 1.0 0.8 BspAI02518-00959 1.0 1.3 1.3BspAI02518-00405 0.9 1.0 0.8 BspAI02518-00412 1.1 2.5 1.4BspAI02518-00590 1.2 2.8 1.3 BspAI02518-00646 1.0 2.0 1.0BspAI02518-01025 1.4 2.8 2.4 BspAI02518-00695 1.0 1.0 0.8BspAI02518-00732 1.4 3.0 1.6 BspAI02518-00772 1.0 1.0 0.9BspAI02518-00802 1.3 6.1 2.4 BspAI02518-00814 1.1 1.1 1.0BspAI02518-00625 1.0 1.0 0.9 BspAI02518-00800 0.9 1.0 0.9BspAI02518-01001 1.3 1.4 1.4 BspAI02518-01032 1.3 1.7 1.3BspAI02518-00594 1.0 1.0 0.6 BspAI02518-00749 1.0 1.0 0.8BspAI02518-00758 1.2 1.4 1.2 BspAI02518-01002 1.1 1.0 1.0BspAI02518-00439 1.0 1.0 0.9

Example 8 Bad02409 Subtilisin Variants with Improved Stability inDetergent

Variants of Bad02409 (SEQ ID NO: 18) subtilisin were evaluated forstability and cleaning performance using methods described in Example 2,and performance index for each variant was calculated versus the parentmolecule.

Table 20 shows the stability results for Bad02409 variants havingstability PI values 1.1 and greater, where the cleaning performanceindex was at least 0.5 or greater (relative to parent) in at least onecleaning assay. Table 21 shows the cleaning assays results for Bad02409variants having cleaning performance PI values 1.0 or greater for atleast one condition when compared to the parent subtilisin, and alsodisplaying stability PI values 1.1 or greater.

TABLE 20 Bad02409 subtilisin variants with improved stability in liquiddetergent at 67° C. (PI values ≥ 1.1) compared to Bad02409 parentSubstitutions in Bad02409 Variant Bad02409 Substitutions in StabilitySample ID numbering BPN′ numbering PI Bad02409-00124 N078D N076D 2.2Bad02409-00592 S080N S078N 1.5 Bad02409-00355 G130S G128S 1.2Bad02409-00369 S185E S182E 1.5 Bad02409-00046 T003V-N221S T003V-N218S1.9 Bad02409-00328 T003V-A071S T003V-A069S 1.8 Bad02409-00360T003V-D262P T003V-D259P 2.3 Bad02409-00398 T003V-M126I T003V-M124I 2.4Bad02409-00449 T003V-N078D T003V-N076D 2.8 Bad02409-00462 T003V-N188QT003V-N185Q 1.4 Bad02409-00543 T003V-G169Q T003V-G166Q 2.0Bad02409-00583 T003V-S080N T003V-S078N 2.0 Bad02409-00634 T003V-S131PT003V-S129P 1.7 Bad02409-00262 A071S-S131P A069S-S129P 1.1Bad02409-00388 A071S-G169Q A069S-G166Q 2.1 Bad02409-00394 A071S-N078DA069S-N076D 2.4 Bad02409-00574 A071S-S080N A069S-S078N 1.9Bad02409-00077 N078D-S131P N076D-S129P 3.0 Bad02409-00566 S080N-N188QS078N-N185Q 2.0 Bad02409-00564 M126I-S131P M124I-S129P 1.2Bad02409-00458 S131P-D262P S129P-D259P 1.6 Bad02409-00567 S131P-G169QS129P-G166Q 1.7 Bad02409-00156 G169Q-N221S G166Q-N218S 1.2

TABLE 21 Bad02409 variants with cleaning performance on par or improvedcompared to Bad02409 parent Cleaning performance PI Bad02409 Variant BMIstain in PNB PAS-38 stain Sample ID detergent In GSM-B detergentBad02409-00124 1.2 1.1 Bad02409-00592 1.1 1.0 Bad02409-00355 1.3 1.0Bad02409-00369 1.0 1.0 Bad02409-00046 1.0 1.0 Bad02409-00328 1.0 1.0Bad02409-00360 1.2 1.1 Bad02409-00398 1.2 1.0 Bad02409-00449 0.9 1.1Bad02409-00462 1.1 1.1 Bad02409-00543 1.5 0.9 Bad02409-00583 1.0 1.0Bad02409-00634 0.9 1.2 Bad02409-00262 1.1 1.1 Bad02409-00388 1.2 1.0Bad02409-00394 1.0 1.0 Bad02409-00574 1.0 1.0 Bad02409-00077 1.0 0.8Bad02409-00566 0.9 1.1 Bad02409-00564 1.1 0.9 Bad02409-00458 0.8 1.2Bad02409-00567 0.8 1.0 Bad02409-00156 1.6 1.0

Example 9 Bba02069 Subtilisin Variants with Improved Stability inDetergent

Variants of Bba02069 (SEQ ID NO: 19) subtilisin were evaluated forstability and cleaning performance using methods described in Example 2,and performance index for each variant was calculated versus the parentmolecule. The Bba02069 subtilisin was previously described as SEQ IDNO:3 in WO 2016/061438 patent application, and is a member of the B.agaradhaerens clade of subtilisins.

Detergent stability results are reported as either performance index(PI) or residual activity (% RA). Tables 22A and 22B show the stabilityresults for Bba02069 variants having stability PI values 1.1 andgreater, where the cleaning performance index was at least 0.5 orgreater (relative to parent) in at least one cleaning assay. Thestability data shown on Table 22 was collected in two separateexperiments, and PI values for certain variants evaluated on bothoccasions showed varying degree of improvements, as can be expected dueto assay to assay fluctuations. Table 23 shows the cleaning assaysresults for Bba02069 variants from Table 22A having cleaning performancePI values 1.0 or greater for at least one condition when compared to theparent subtilisin, and also displaying stability PI values 1.1 orgreater.

TABLE 22A Bba02069 subtilisin variants with improved stability in liquiddetergent at 40° C. (PI values ≥ 1.1) compared to Bba02069 parentSubstitutions in Bba02069 Variant Bba02069 Substitutions in StabilitySample ID numbering BPN′ numbering PI Bba02069-00641 S129P S129P 1.3Bba02069-00642 G118R G118R 1.5 Bba02069-00643 Q087D Q087D 1.5Bba02069-00644 N076D N076D 3.2 Bba02069-00646 M124I M124I 2.6Bba02069-00647 Q249D Q248D 1.4 Bba02069-00648 A069S A069S 1.9Bba02069-00649 G128S G128S 1.5 Bba02069-00650 N024Q N024Q 1.1Bba02069-00652 Q003V Q003V 2.0 Bba02069-00653 P040E P040E 1.3Bba02069-00654 T009E T009E 2.3 Bba02069-00655 N219S N218S 3.1Bba02069-00111 G167Q G166Q 2.0 Bba02069-00217 S260P S259P 1.7Bba02069-00030 Q003V-A069S Q003V-A069S 2.0 Bba02069-00121 Q003V-V186QQ003V-V185Q 2.0 Bba02069-00203 Q003V-S129P Q003V-S129P 2.0Bba02069-00291 Q003V-M124I Q003V-M124I 2.8 Bba02069-00347 Q003V-G167QQ003V-G166Q 3.9 Bba02069-00400 Q003V-G128S Q003V-G128S 2.4Bba02069-00477 Q003V-S260P Q003V-S259P 3.2 Bba02069-00564 Q003V-N076DQ003V-N076D 2.4 Bba02069-00377 P040E-V186Q P040E-V185Q 1.8Bba02069-00499 P040E-G167Q P040E-G166Q 3.1 Bba02069-00007 A069S-G128SA069S-G128S 1.8 Bba02069-00114 A069S-S260P A069S-S259P 2.1Bba02069-00116 A069S-M124I A069S-M124I 2.2 Bba02069-00505 A069S-G167QA069S-G166Q 2.5 Bba02069-00518 A069S-N076D A069S-N076D 3.0Bba02069-00118 N076D-G128S N076D-G128S 2.4 Bba02069-00247 N076D-G167QN076D-G166Q 3.0 Bba02069-00281 N076D-M124I N076D-M124I 3.1Bba02069-00423 N076D-S260P N076D-S259P 2.5 Bba02069-00473 N076D-S129PN076D-S129P 3.2 Bba02069-00037 M124I-G128S M124I-G128S 1.9Bba02069-00254 M124I-V186Q M124I-V185Q 1.8 Bba02069-00390 M124I-S129PM124I-S129P 2.3 Bba02069-00461 M124I-S260P M124I-S259P 3.2Bba02069-00465 M124I-G167Q M124I-G166Q 2.7 Bba02069-00568 M124I-N219SM124I-N218S 3.3 Bba02069-00223 G128S-S129P G128S-S129P 1.5Bba02069-00399 G128S-G167Q G128S-G166Q 2.6 Bba02069-00429 G128S-S260PG128S-S259P 2.4 Bba02069-00483 G128S-V186Q G128S-V185Q 1.6Bba02069-00008 S129P-G167Q S129P-G166Q 2.1 Bba02069-00133 S129P-V186QS129P-V185Q 1.4 Bba02069-00274 S129P-S260P S129P-S259P 1.8Bba02069-00043 G167Q-S260P G166Q-S259P 2.6 Bba02069-00190 G167Q-V186QG166Q-V185Q 2.1 Bba02069-00005 V186Q-S260P V185Q-S259P 2.1Bba02069-00493 V186Q-N219S V185Q-N218S 1.6 Bba02069-00051 N219S-S260PN218S-S259P 1.9

TABLE 22B Bba02069 subtilisin variants with improved stability in liquiddetergent at 39° C. (reported as percent residual activity, % RA)compared to Bba02069 parent Substitutions in Bba02069 Variant Bba02069Substitutions in Sample ID numbering BPN′ numbering % RA Bba02069 — — 23Bba02069-00854 Q003V-T009E Q003V-T009E 87 Bba02069-00855 Q003V-P040EQ003V-P040E 56 Bba02069-00856 Q003V-N219S Q003V-N218S 74 Bba02069-00755T009E-P040E T009E-P040E 72 Bba02069-00756 T009E-A069S T009E-A069S 70Bba02069-00757 T009E-N076D T009E-N076D 100 Bba02069-00871 T009E-G167QT009E-G166Q 76 Bba02069-00866 T009E-V186Q T009E-V185Q 67 Bba02069-00865T009E-N219S T009E-N218S 84 Bba02069-00758 T009E-S260P T009E-S259P 90Bba02069-00863 P040E-A069S P040E-A069S 41 Bba02069-00824 P040E-N076DP040E-N076D 77 Bba02069-01952 P040E-N219S P040E-N218S 59 Bba02069-00845P040E-S260P P040E-S259P 64 Bba02069-00844 A069S-V186Q A069S-V185Q 31Bba02069-00736 A069S-N219S A069S-N218S 61 Bba02069-00822 N076D-V186QN076D-V185Q 74 Bba02069-00815 N076D-N219S N076D-N218S 80 Bba02069-00817G167Q-N219S G166Q-N218S 68

TABLE 23 Bba02069 variants with cleaning performance on par or improvedcompared to Bba02069 parent Cleaning performance PI PAS-38 in Bba02069Variant BMI in PNB GSM-B BMI in ECE-2 Sample ID detergent detergentdetergent Bba02069-00111 0.8 1.0 0.9 Bba02069-00217 1.0 0.9 0.9Bba02069-00121 0.8 1.0 1.0 Bba02069-00203 1.1 1.1 1.0 Bba02069-00291 0.71.4 0.8 Bba02069-00400 0.7 1.0 0.8 Bba02069-00377 1.2 1.0 0.8Bba02069-00499 1.0 0.9 0.8 Bba02069-00114 1.1 0.9 1.1 Bba02069-00116 0.91.3 0.9 Bba02069-00505 1.0 0.8 0.9 Bba02069-00518 1.1 0.9 0.8Bba02069-00118 1.1 1.0 1.0 Bba02069-00247 1.1 0.9 0.8 Bba02069-00281 1.51.1 0.7 Bba02069-00423 1.1 0.8 1.1 Bba02069-00473 1.2 0.9 1.2Bba02069-00037 1.3 1.2 0.8 Bba02069-00254 1.1 1.2 0.7 Bba02069-00390 0.71.2 0.8 Bba02069-00461 0.9 1.1 0.9 Bba02069-00465 1.0 1.0 0.7Bba02069-00568 0.9 1.1 0.6 Bba02069-00223 1.0 1.0 1.0 Bba02069-00399 1.00.9 0.8 Bba02069-00429 0.7 1.0 0.8 Bba02069-00483 0.9 0.9 1.0Bba02069-00133 1.1 0.9 1.0 Bba02069-00274 1.2 1.0 1.2 Bba02069-00043 1.00.8 0.9 Bba02069-00190 0.8 1.0 0.9

Example 10 BspZ00056 Subtilisin Variants with Improved Stability inDetergent

Variants of BspZ00056 (SEQ ID NO: 17) subtilisin were evaluated forstability and cleaning performance using methods described in Example 2,and performance index for each variant was calculated versus the parentmolecule. The BspZ00056 subtilisin was previously described as SEQ IDNO: 9 in WO 2016/069544 patent application, and is a member of theBspAP02013 clade of subtilisins.

Detergent stability results are reported as either performance index(PI) or residual activity (% RA). Tables 24A and 24B show the stabilityresults for BspZ00056 variants having stability PI values 1.1 andgreater, where the cleaning performance index was at least 0.5 orgreater (relative to parent) in at least one cleaning assay. Table 25shows the cleaning assays results for BspZ00056 variants from Table 24Ahaving cleaning performance PI values 1.0 or greater for at least onecondition when compared to the parent subtilisin, and also displayingstability PI values 1.1 or greater. PI values of less than 0.5 aredenoted as <0.5.

TABLE 24A BspZ00056 subtilisin variants with improved stability inliquid detergent at 63° C. (PI values > 1.1) compared to BspZ00056parent Substitutions in BspZ00056 Variant BspZ00056 Substitutions inStability Sample ID numbering BPN′ numbering PI BspZ00056-00354 Q187EQ182E 1.2 BspZ00056-00177 G132S G128S 1.7 BspZ00056-00408 E149R E145R1.5 BspZ00056-00191 M128I M124I 1.7 BspZ00056-00248 N223S N218S 1.1BspZ00056-00380 S133P S129P 1.5 BspZ00056-00022 G132S-S133P G128S-S129P1.5 BspZ00056-00005 G132S-N223S G128S-N218S 1.9 BspZ00056-00042A073S-N190Q A069S-N185Q 1.1 BspZ00056-00490 A073S-D082N A069S-D078N 1.2BspZ00056-00297 D082N-G171Q D078N-G166Q 1.5 BspZ00056-00257 G171Q-N190QG166Q-N185Q 2.0 BspZ00056-00357 T003V-M128I T003V-M124I 2.1BspZ00056-00294 G132S-N190Q G128S-N185Q 1.5 BspZ00056-00492 A073S-G132SA069S-G128S 2.0 BspZ00056-00259 M128I-N190Q M124I-N185Q 1.8BspZ00056-00133 G171Q-G264P G166Q-G259P 2.1 BspZ00056-00151 A073S-G264PA069S-G259P 1.9 BspZ00056-00288 S133P-G171Q S129P-G166Q 2.1BspZ00056-00384 T003V-G264P T003V-G259P 2.1 BspZ00056-00116 T003V-N190QT003V-N185Q 1.1 BspZ00056-00088 D082N-G264P D078N-G259P 1.7BspZ00056-00092 M128I-N223S M124I-N218S 1.8 BspZ00056-00451 G132S-G171QG128S-G166Q 2.1 BspZ00056-00324 A073S-M128I A069S-M124I 2.2BspZ00056-00207 S133P-N190Q S129P-N185Q 1.4 BspZ00056-00135 G132S-G264PG128S-G259P 2.2 BspZ00056-00221 T003V-G171Q T003V-G166Q 2.1BspZ00056-00359 T003V-G132S T003V-G128S 1.8 BspZ00056-00094 T003V-A073ST003V-A069S 1.2 BspZ00056-00422 M128I-G171Q M124I-G166Q 2.2BspZ00056-00429 M128I-S133P M124I-S129P 2.0 BspZ00056-00491 N223S-G264PN218S-G259P 1.9 BspZ00056-00377 N190Q-G264P N185Q-G259P 1.9BspZ00056-00399 D082N-S133P D078N-S129P 1.1 BspZ00056-00201 M128I-G132SM124I-G128S 1.7 BspZ00056-00368 T003V-N223S T003V-N218S 1.4BspZ00056-00389 A073S-G171Q A069S-G166Q 2.2

TABLE 24B BspZ00056 subtilisin variants with improved stability inliquid detergent at 64° C. (reported as percent residual activity, % RA)compared to BspZ00056 parent Substitutions in BspZ00056 VariantBspZ00056 Substitutions in Sample ID numbering BPN′ numbering % RABspZ00056 — — 30 BspZ00056-00876 T003V T003V 35 BspZ00056-01485 P009EP009E 33 BspZ00056-00863 A073S A069S 42 BspZ00056-00864 G171Q G166Q 69BspZ00056-00663 N190Q N185Q 38 BspZ00056-00819 G264P G259P 80BspZ00056-01478 P009E-G171Q P009E-G166Q 69 BspZ00056-00875 P009E-G264PP009E-G259P 83 BspZ00056-00873 A073S-N223S A069S-N218S 44BspZ00056-00837 G171Q-N223S G166Q-N218S 80 BspZ00056-01030 N190Q-N223SN185Q-N218S 35

TABLE 25 BspZ00056 variants with performance on par or improved comparedto BspZ00056 parent Cleaning performance PI BspZ00056 Variant BMI stainin PNB PAS-38 stain in Sample ID detergent GSM-B detergentBspZ00056-00354 1.1 0.8 BspZ00056-00022 1.2 0.9 BspZ00056-00005 1.2 0.9BspZ00056-00042 1.1 0.7 BspZ00056-00490 1.1 0.9 BspZ00056-00297 1.0 1.4BspZ00056-00257 1.0 1.3 BspZ00056-00357 1.0 <0.5 BspZ00056-00294 1.0 0.9BspZ00056-00492 1.0 0.5 BspZ00056-00133 1.0 1.4 BspZ00056-00288 0.9 1.2BspZ00056-00088 0.9 1.0 BspZ00056-00451 0.8 1.2 BspZ00056-00207 0.9 1.1BspZ00056-00221 0.9 1.4 BspZ00056-00389 0.6 1.0

Example 11 BspAK01305 Subtilisin Variants with Improved Stability inDetergent

Variants of BspAK01305 (SEQ ID NO: 15) subtilisin were evaluated forstability and cleaning performance using methods described in Example 2,and performance index for each variant was calculated versus the parentmolecule. The BspAK01305 subtilisin was previously described as SEQ IDNO:6 in WO 2016/069569 patent application, and is a member of theBspAL03279 clade of subtilisins.

Table 26 shows the stability results for BspAK01305 variants havingstability PI values 1.1 and greater, where the cleaning performanceindex was at least 0.5 or greater (relative to parent) in at least onecleaning assay. Table 27 shows the cleaning assays results forBspAK01305 variants having cleaning performance PI values 1.0 or greaterfor at least one condition when compared to the parent subtilisin, andalso displaying stability PI values 1.1 or greater.

TABLE 26 BspAK01305 subtilisin variants with improved stability inliquid detergent at 47° C. (PI values ≥ 1.1) compared to BspAK01305parent Substitutions in BspAK01305 Variant BspAK01305 Substitutions inStability Sample ID numbering BPN′ numbering PI BspAK01305-00530 S003VS003V 1.5 BspAK01305-00444 S039E S040E 1.5 BspAK01305-00325 G160Q G166Q1.7 BspAK01305-00495 S179Q S185Q 1.4 BspAK01305-00060 P204I P210I 1.9BspAK01305-00509 S003V-S179Q S003V-S185Q 1.9 BspAK01305-00514S003V-G160Q S003V-G166Q 1.7 BspAK01305-00538 S003V-R256L S003V-R262L 1.5BspAK01305-00564 S003V-S039E S003V-S040E 1.7 BspAK01305-00027S039E-G160Q S040E-G166Q 2.3 BspAK01305-00264 S039E-S179Q S040E-S185Q 1.8BspAK01305-00316 G160Q-S179Q G166Q-S185Q 2.2

TABLE 27 BspAK01305 variants with performance on par or improvedcompared to BspAK01305 parent Cleaning performance PI BspAK01305 VariantBMI stain in PNB PAS-38 stain in Sample ID detergent GSM-B detergentBspAK01305-00530 0.9 1.1 BspAK01305-00444 0.9 1.5 BspAK01305-00325 1.12.2 BspAK01305-00060 1.1 1.1 BspAK01305-00514 0.9 1.8 BspAK01305-005641.3 1.2 BspAK01305-00027 0.6 1.0 BspAK01305-00264 1.0 0.9BspAK01305-00316 0.6 1.2

Example 12 Sequence Comparison and Structural Features of SubtilisinSites Providing Enhanced Stability

A multiple sequence alignment of the mature (in some cases predicted)polypeptide regions of the subtilisin backbones evaluated in this study,as well as other subtilisins was generated using the followingsequences: AprE (subtilisin E, SEQ ID NO:8); WP_082194748 (SEQ ID NO:9); Chemgen_164A (SEQ ID NO:10); CP474 (SEQ ID NO:11); ZP-00454 (SEQ IDNO:12); Bpan01744 (SEQ ID NO:13); DSM14391 (SEQ ID NO:14); BspAK01305(SEQ ID NO:15); BspAI02518 (SEQ ID NO:16); BspZ00056 (SEQ ID NO:17);Bad02409 (SEQ ID NO:18); Bba02069 (SEQ ID NO:19); BspZ00258 (SEQ IDNO:22); BPN′ (SEQ ID NO:1); B. licheniformis AprL (SEQ ID NO:2); B.lentus GG36 (SEQ ID NO:3); B. gibsonii Bgi02446 (SEQ ID NO:4); andBacillus sp LG12 (SEQ ID NO:6). The multiple protein sequencealignments, shown in Table 28, were generated using structural (mainchain) alignments from available protein crystal structures and aminoacid sequence homology to guide positioning of loops in the sequences,and using BPN′ numbering (as assigned to all variants in thisapplication, and used in the Examples above). Positions where insertionswould occur using BPN′ sequence as a reference are numbered according toBPN′ and a suffix (example: position 42, 42a, 42b). The alignments showncorrespond to residues 1-275 of BPN′, and additional C-terminal residuesin some subtilisin backbones are not shown. An empty cell corresponds toa position where no amino acid can be assigned for that particularsubtilisin sequence. The subtilisins on Table 28 with an asterisk (*)denote backbones not evaluated in this study, and shown here forreference.

TABLE 28Structure-based multiple sequence alignment of various subtilisins. BPN′numbering *BPN′ AprE WP_082194748 *AprL *LG12 Chemgen_164A CP474ZP-00454 *GG36   1 A A A A A A A A A   2 Q Q Q Q Q Q Q Q Q   3 S S T T TT T V S   4 V V V V V T V V V   5 P P P P P P P P P   6 Y Y Y Y W W W WW   7 G G G G G G G G G   8 V I I I I I I I I   9 S S P P P T P P S  10Q Q Q L H H H H R  11 I I I I I I I I V  12 K K K K K N K K Q  13 A A AA A A A A A  14 P P P D D H D D P  15 A A A K K K K K A  16 L L V V A AA A A  17 H H H Q H H H H H   17a  18 S S A A A S A A N  19 Q Q Q Q A SA S R  20 G G G G G S G G G  21 Y Y Y F V V V V L  22 T T K K T T T T T 23 G G G G G G G G G  24 S S A A S S S S S  25 N N N N G G G G G  26 VV V V V V V V V  27 K K K K K K K K K  28 V V V V V V V V V  29 A A A AA A A A A  30 V V V V I V I V V  31 L L L L L L L L L  32 D D D D D D DD D  33 S S T T T T T T T  34 G G G G G G G G G  35 I I I I I I I I I 36 D D H Q D D D D S  37 S S A A A A A A  38 S S A S N S N N T  39 H HH H H H H H H  40 P P P P A P A A P  41 D D D D D D D D D  42 L L L L LL L L L   42a   42b  43 K N N N N N N N N  44 V V V V V V V V I  45 A RA V K K K K R  46 G G G G G G G G G  47 G G G G G G G G G  48 A A A A AA A A A  49 S S S S S S S S S  50 M F F F F F F F F  51 V V V V V I V VV  52 P P P A S S A S P  53 S S S G G G G G G  54 E E E E E E E E E  55T T P P P P P P  56 N N N A N N N N S   56a   56b  57 P P A Y A A A A 58 F Y T N L L L L T  59 Q Q Q T Q V Q Q Q  60 D D D D D D D D D  61 NG F G G T G G G  62 N S Q N N N N N N  63 S S S G G G G G G  64 H H H HH H H H H  65 G G G G G G G G G  66 T T T T T T T T T  67 H H H H H H HH H  68 V V V V V V V V V  69 A A A A A A A A A  70 G G G G G G G G G 71 T T T T T T T T T  72 V I I V V V V V I  73 A A A A A A A A A  74 AA A A A A A A A  75 L L L L L L L L L  76 N N D D N N D N N  77 N N N NN N N N N  78 S S T T T T T T S  79 I I I T T I T T I  80 G G G G G G GG G  81 V V V V V V V V V  82 L L L L L V L L L  83 G G G G G G G G G 84 V V V V V V V V V  85 A A A A A A A A A  86 P P P P Y Y P Y P  87 SS S S N N S N S  88 A A A V A A V A A  89 S S S S D D S F E  90 L L L LL L L L L  91 Y Y Y Y Y Y Y Y Y  92 A A A A A A A A A  93 V V V V V V VV V  94 K K K K K K K K K  95 V V V V V V V V V  96 L L L L L L L L L 97 G D D N S S G G G  98 A S R S A A A A A  99 D T N S S S S S S 100 GG G G G G G G G 101 S S D S S S S S S 102 G G G G G G G G G 103 Q Q Q ST T S T S 104 Y Y Y Y L L V L V 105 S S S S S S S S S 106 W W W G G G SG S 107 I I I I I I I I I 108 I I I V A A A A A 109 N N S S Q Q Q Q Q110 G G G G G G G G G 111 I I I I I V L I L 112 E E E E E E E E E 113 WW W W W W W W W 114 A A A A S A A S A 115 I I V T I I G I G 116 A S A TS A N A N 117 N N N N N N N N N 118 N N N G G N G D G 119 M M M M M M MM M 120 D D D D N D H D H 121 V V V V V V V V V 122 I I I I I I A I A123 N N N N N N N N N 124 M M M M M M L M L 125 S S S S S S S S S 126 LL L L L L L L L 127 G G G G G G G G G 128 G G G G G G S I S 129 P P P AS S P S P 130 S T S S S S S T S 131 G G G G G G P G P 132 S S S S S S SS S 133 A T T T T T A T A 134 A A A A A A T A T 135 L L L M L L L L L136 K K K K Q K E Q E 137 A T N Q Q Q Q Q Q 138 A V A A A A A A A 139 VV V V C V V C V 140 D D D D N D N N N 141 K K T N N N S N S 142 A A A AA A A A A 143 V V N Y Y Y T Y T 144 A S N A N A S A S 145 S S R R R S RS R 146 G G G G G G G G G 147 V I V V I I V I V 148 V V V V V V L V L149 V V V V V V V V V 150 V A V V I V V V V 151 A A A A S A A A A 152 AA A A S A A A A 153 A A A A A A S A S 154 G G G G G G G G G 155 N N N NN N N N N 156 E E S S S S S S S 157 G G G G G G G G G 158 T S S S S T AS A  158a 159 S S S S S R N 160 G G G G G G G G G 161 S S S N N R K 162S T T T R Q R 163 S S S N N N N 164 T T T T T T S T S 165 V V V I M M IM I 166 G G G G G G S G S 167 Y Y Y Y Y Y Y Y Y 168 P P P P P P P P P169 A A A A A A A A A 170 K K K K R R R R R 171 Y Y Y Y Y Y Y Y Y 172 PP D D S S A S A 173 S S S S S S N S N 174 V T T V V V A V A 175 I I I II I M I M 176 A A A A A A A A A 177 V V V V V V V V V 178 G G A G G G GG G 179 A A N A A A A A A 180 V V V V V V T V T 181 D N N D S D D D D182 S S S S S S Q S Q 183 S S N N N N N S N 184 N N N S N N N N N 185 QQ V N T N N N N 186 R R R R R R R R R 187 A A N A A A A A A 188 S S S SS S S S S 189 F F S F F F F F F 190 S S S S S S S S S 191 S S S S S S QS Q 192 V A A V V V Y V Y 193 G G G G G G G G G 194 P S P A S A A S A195 E E E E E E G E G 196 L L L L L L L L L 197 D D D E E E D E D 198 VV V V V V I V I 199 M M S M M M V M V 200 A A A A A A A A A 201 P P P PP P P P P 202 G G G G G G G G G 203 V V T A V V V V V 204 S S S G N S NS N 205 I I I V I V I I V 206 Q Q L Y L L L L Q 207 S S S S S S S S S208 T T T T T T T T T 209 L L V Y T V T T Y 210 P P P P P P P P P 211 GG S T G G G G G 212 N G S N N G N N S 213 K T G T N G N N T 214 Y Y Y YY Y Y Y Y 215 G G A A A A A E A 216 A A S T S S S S S 217 Y Y Y L F Y LF L 218 N N T N N N N N N 219 G G G G G G G G G 220 T T T T T T T T T221 S S S S S S S S S 222 M M M M M M M M M 223 A A A A A A A A A 224 ST S S A S A S T 225 P P P P P P P P P 226 H H H H H H H H H 227 V V V VV V V V V 228 A A A A A A A A A 229 G G G G G G G G G 230 A A A A A A AA A 231 A A A A A A A A A 232 A A A A A A A A A 233 L L L L L L L L L234 I I I I I I I I V 235 L L L L K K K K K 236 S S S S A A A A Q 237 KK K K K K K K K 238 H H H H Y Y Y Y N 239 P P P P P P P P P 240 N T N NS S S S S 241 W W L L M L M M W 242 T T T S T S T T S 243 N N N A N A NN N 244 T A T S V S V V V 245 Q Q Q Q Q Q Q Q Q 246 V V V V I I I I I247 R R R R R R R R R 248 S D Q N E D N N N 249 S R R R R R R K H 250 LL L L L L L L L 251 E E E S K R K K K 252 N S N S N N N N N 253 T T T TT T T T T 254 T A A A A A A A A 255 T T T T T T T T T 256 K Y P Y N Y NN S 257 L L L L L L L L L 258 G G G G G G G G G 259 D N S S D D D D S260 S S S S P P P A T 261 F F F F F F F F N 262 Y Y Y Y F Y F Y L 263 YY Y Y Y Y Y Y Y 264 G G G G G G G G G 265 K K K K K N K H S 266 G G G GG G G G G 267 L L L L V V V V L 268 I I I I I I I I V 269 N N N N N N NN N 270 V V V V V V V V A 271 Q Q Q E E E E E E 272 A A A A S R S K A273 A A A A A A A A A 274 A A A A L L L L T 275 Q Q N Q Q Q Q Q R BPN′numbering Bpan01744 *Bgi02446 DSM14391 BspAK01305 BspZ00258 BspAI02518BspZ00056 Bad02409 Bba02069   1 A Q Q A A A G A Q   2 Q Q Q Q Q Q Q Q Q  3 S T T S E S T T Q   4 V V V I V T V V T   5 P P P P P P P P P   6 WW W W Y W W W W   7 G G G G G G G G G   8 I I I I I I I V I   9 S T T EE S P P T  10 R R R R Q R H H R  11 V V V I I I V V V  12 Q Q Q G G N QQ Q  13 A A A T A A G G G  14 Q P P P I P T T I  15 S A T A D A A D A 16 A V V A V V A A A  17 H H H H Q H Q H Q   17a V  18 N N N A N S D AS  19 R R R S D T A A Q  20 G G G G G G G G G  21 I I I F N N Y H Y  22T T T T T F T T T  23 G G G G G G G G G  24 S S S S N Q A S N  25 G G GG G G G G N  26 V V V V V V L V V  27 K R K S S R K K K  28 V V V V V VV V V  29 A A A A A A A A A  30 V I I V V V I I V  31 L L L L L L L L L 32 D D D D D D D D D  33 T S T T T S T T S  34 G G G G G G G G G  35 II I I I V I I I  36 S S A D A A D D D  37 R R R  38 T A Q P A S N N S 39 H H H H H H H H H  40 E S S S E E E E P  41 D D D D D D D D D  42 LL L L L L L L L   42a F S   42b A A  43 N N T N N R N N N  44 V I I V VI V V V  45 R R R Q V A K R R  46 G G G G D G G G G  47 G G G G G G G GG  48 A A A V A V H H Y  49 S S S S S S S S S  50 F F F F F F V V V  51V V V V I V F F F  52 A P P P A A T T G  53 G G G G G S D D D  54 E E EE E E S S S  55 P P S S P P A A P  56 G T T G D S N N   56a S R   56b DD  57 P P  58 Y T T A Y Y F Y Y  59 Q A A D E Q Y Y N  60 D D D D D D DD D  61 G L L G Y Y A G G  62 N N N N N N D S N  63 G G G G G G G G G 64 H H H H H H H H H  65 G G G G G G G G G  66 T T T T T T T T T  67 HH H H H H H H H  68 V V V V V V V V V  69 A A A A A A A A A  70 G G G GG G G G G  71 T T T T T T T T T  72 I V V I V I V V V  73 A A A A A A AA G  74 A A A A A G A A A  75 L L L L L L V L V  76 N N N D D N D N N 77 N N N N N N N N N  78 S S S D D S D S N  79 I I I E L V L V I  80 GG G G D G G G G  81 V V V V V V V V V  82 L I I L L L V L I  83 G G G GG G G G G  84 V V V V V V V V V  85 A A A A S A A A A  86 P P P P P P SY P  87 N N S E D S Q N Q  88 A A A V V V A A A  89 E E D D D Q E E D 90 L L L L L L L L V  91 L Y Y F Y Y Y Y Y  92 A A A A A A A A A  93 VV V V V V V V V  94 K K K K K K K K K  95 V V V V V V V V V  96 L L L LL L L L L  97 G G G S G D N N N  98 A A A A A R N N N  99 S N N S D N SS S 100 G G G G G G G G G 101 S S R S G G S S S 102 G G G G G G G G G103 S S S S S N S S S 104 I V V I H H Y Y Y 105 S S S S A S A A A 106 GG G S S D G G G 107 I I I I I I I I I 108 A A A A A A A A A 109 Q Q Q QQ R E E Q 110 G G G G G G G G G 111 L L L L I I I I I 112 Q E E E E E EE E 113 W W W W Y W W W W 114 A A A T A S S A S 115 G A A A V V I V I116 N T T E D N N N N 117 N N N N N N N N N 118 G N N N N G G G G 119 MM M I I M M M M 120 H H H D D H D D D 121 I I I V V V I I I 122 A A A AV V I I I 123 N N N N N N N N N 124 M M M L M M M M M 125 S S S S S S SS S 126 L L L L L L L L L 127 G G G G G G G G G 128 T S S S G G G G G129 S D D P A P S S S 130 A F A S V T Q M S 131 P P P P G G S S S 132 SS S S S S S S S 133 A S T Q T T S S S 134 T T T T T T I I I 135 L L L LL L L L L 136 E E E E E Q K E E 137 Q R R Q Q R Q E Q 138 A A A A A A FW Y 139 V V V V V A S C C 140 N N N N N D D N N 141 A Y Y D Y N L I L142 A A A A A A A A A 143 T T T T H Y Y Y Y 144 S S S D S N E N N 145 RR R S Q R E S R 146 G D G G G G G G G 147 V V V V V V L V L 148 L L L LT L L L L 149 V V V V L L V V V 150 I I I V I I V V V 151 A A A A A A AA A 152 A A A A A A A A A 153 S T T A A A A A A 154 G G G G G G G G G155 N N N N N N N N N 156 S N N S E T S S S 157 G G G G G G G G G 158 AS T T S T N R T  158a L R T A 159 S I S G N A 160 G G G P G G G 161 G NR N 162 L N G T 163 N D D N 164 S S S S T G T T T 165 V V I L I V V V V166 G G G G G S G G G 167 Y Y Y Y Y F Y Y Y 168 P P P P P P P P P 169 AA A A A A A A A 170 R R R R K R K K R 171 Y Y Y Y Y Y Y Y Y 172 A A A DD S D D N 173 N N N N N S S S S 174 A A A A V V V V V 175 M M M M I M II I 176 A A A A A A A A A 177 V V V V V V V V V 178 G G G G G A A A A179 A A A A A A A A A 180 T T T T V T V V T 181 D D D D D D D D N 182 QQ Q Q S S Q S S 183 N N N S N N N S N 184 N N N D N N N N N 185 N R R SN N N N V 186 R R R L R R R R R 187 A A A A A A A A G 188 S N S S S S TS N 189 F F F F F F F F F 190 S S S S S S S S S 191 Q Q Q Q S T S S S192 Y Y Y Y V Y T T T 193 G G G G G G G G G 194 A T T E N S P P P 195 GG G G E Q A A T 196 L I I L L I V V V 197 D D D D D E E E E 198 I I I LV I I I L 199 V V V V V S S A S 200 A A A A A A A A A 201 P P P P P P PP P 202 G G G G G G G G G 203 V V V V V V V V V 204 G N G G S G S N S205 V V I V I I I I V 206 Q Q Q E L N L L L 207 S S S S S S S S S 208 TT T T T T T T T 209 Y Y Y Y Y Y T T T 210 P P L P L P P P P 211 G G N GG T G G G 212 N N N G N N N N G 213 R R S G D G N S N 214 Y Y Y Y Y Y YY Y 215 A V A D A S A A A 216 S S S S A S A S S 217 L M M L L L F Y Y218 N N N P S N N N N 219 G G G G G G G G G 220 T T T T T T T T T 221 SS S S S S S S S 222 M M M M M M M M M 223 A A A A A A A A A 224 T T T AS S S S S 225 P P P P P P P P P 226 H H H H H H H H H 227 V V V V V V VV V 228 A A A A A A A A A 229 G G G G G G G G G 230 V A V A A V V V V231 A A A A A A A A A 232 A A A A A A A A A 233 L L L L L L Q L Q 234 VV V V L V V V V 235 K K K K L K W L W 236 Q Q Q Q A A Q A Q 237 K R K KE R A A A 238 N Y N N N Y K N R 239 P P P P P P P P P 240 S S S G G S EN N 241 W W W W L A L L L 242 S N N T T T S S S 243 N A A N N N N N N244 V T T E D A V V A 245 Q Q Q Q Q Q E E Q 246 V I I I V I L L L 247 RR R R R R R R R 248 N N N S A Q N N Q 249 H H H H V H L R I 250 L L L LF L L L L 251 K K K N N R N N N 252 N N N D E S E D A 253 T T T T T T TT S 254 A A A A A S A A A 255 T T T N V T V Q Q 256 N N N D P Y N N N257 L L L L L L L L L 258 G G G G G G G G G 259 N N N D D N G D S 260 TS S S H S S A S 261 N S S F F T N N Y 262 L Q Q R Y Y Q H Q 263 Y F F FY Y F F Y 264 G G G G G G G G G 265 S S S S N S H N N 266 G G G G G G GG G 267 L L L L L L L L L 268 V V V L I V V V V 269 N N N N D D Q R R270 A A A A V A S A S 271 E E D E R Q L V L 272 A A A N A R D D N 273 AA A A A A A A A 274 T T T V I T I I I 275 R R R Q D N Q N Q

The percent identity for the mature (in some cases predicted) amino acidsequences of the subtilisins (corresponding to residues 1-275 of BPN′)was calculated based on the alignment shown on Table 28, using theMUSCLE (Geneious version 10.2.6) software, and results are shown onTable 29.

TABLE 29 Percent identity over the mature amino acid sequence ofmultiple subtilisins. BPN′ AprE WP_082194748 AprL LG12 Chemgen′164ACP474 ZP-00454 GG36 Bpan01744 BPN′ 100 86.5 76.4 69.5 65.1 68 60.7 68 6058.2 AprE 86.5 100 77.5 69.8 65.8 66.5 58.9 66.5 60.4 59.3 WP_08219474876.4 77.5 100 73.8 65.8 66.2 61.5 64.7 58.5 55.3 AprL 69.5 69.8 73.8 10070.9 72 66.5 70.2 61.1 60.4 LG12 65.1 65.8 65.8 70.9 100 81.8 79.6 90.263.3 64.4 Chemgen_164A 68 66.5 66.2 72 81.8 100 69.8 82.9 62.5 62.2CP474 60.7 58.9 61.5 66.5 79.6 69.8 100 76 81.2 76.8 ZP-00454 68 66.564.7 70.2 90.2 82.9 76 100 63.3 64.4 GG36 60 60.4 58.5 61.1 63.3 62.581.2 63.3 100 89.6 Bpan01744 58.2 59.3 55.3 60.4 64.4 62.2 76.8 64.489.6 100 Bgi02446 56 56 54.2 54.9 60 58.5 69.7 58.9 79.9 80.3 DSM1439155.6 54.9 54.5 55.6 58.9 57.8 69.4 57.5 78.4 79.2 BspAK01305 56.7 5654.2 57.1 59.3 60 69.5 60 72.2 69.3 BspZ00258 60.6 59.2 60.6 64.6 6161.7 61 62.1 58.2 59.6 BspAI02518 57.1 58.5 58.5 57.1 58.9 58.2 58.858.5 63.3 63.3 BspZ00056 53.6 52.1 53.6 57.1 60 57.5 56.1 60 53.2 56.1Bad02409 57.6 56.5 56.8 58.6 64.7 61.5 60.4 65.1 58.6 62.2 Bba02069 55.456.1 56.5 57.9 60.1 61.5 53.6 58.6 57 58.5 Bgi02446 DSM14391 BspAK01305BspZ00258 BspAI02518 BspZ00056 Bad02409 Bba02069 BPN′ 56 55.6 56.7 60.657.1 53.6 57.6 55.4 AprE 56 54.9 56 59.2 58.5 52.1 56.5 56.1WP_082194748 54.2 54.5 54.2 60.6 58.5 53.6 56.8 56.5 AprL 54.9 55.6 57.164.6 57.1 57.1 58.6 57.9 LG12 60 58.9 59.3 61 58.9 60 64.7 60.1Chemgen_164A 58.5 57.8 60 61.7 58.2 57.5 61.5 61.5 CP474 69.7 69.4 69.561 58.8 56.1 60.4 53.6 ZP-00454 58.9 57.5 60 62.1 58.5 60 65.1 58.6 GG3679.9 78.4 72.2 58.2 63.3 53.2 58.6 57 Bpan01744 80.3 79.2 69.3 59.6 63.356.1 62.2 58.5 Bgi02446 100 90 65.6 55.6 61.1 52.5 56.1 56 DSM14391 90100 65.9 57.1 61.1 51.4 55.8 53.8 BspAK01305 65.6 65.9 100 58.9 57.249.3 53.6 53.1 BspZ00258 55.6 57.1 58.9 100 57.1 53.2 56.2 52.7BspAI02518 61.1 61.1 57.2 57.1 100 49.3 54 54.2 BspZ00056 52.5 51.4 49.353.2 49.3 100 77.2 72.2 Bad02409 56.1 55.8 53.6 56.2 54 77.2 100 69Bba02069 56 53.8 53.1 52.7 54.2 72.2 69 100

An analysis of available crystal structures and homology models ofseveral of the subtilisin proteases evaluated in this study or theirclose homologs was performed. The three-dimensional structures orhomology models of six subtilisins: the B. subtilis (strain 168)subtilisin E (AprE) Protein Data Bank (PDB) entry 1SCJ; the Bacillus sp.subtilisin LG12 SprC (LG12) homology model described in WO2015038792;the B. amyloliquefaciens (BPN′) PDB entry 2ST1; the B. licheniformis(AprL) PDB entry 1CSE; B. lentus (GG36) PDB entry 1JEA; and the B.gibsonii DSM14391 subtilisin homology model (based on B. gibsonii-cladeBSP-00801 structure described in WO2016205755) were used to examinesites where globally beneficial substitutions were evaluated andidentified. The superposition of the main chain fold of thesesubtilisins (image not shown) indicates that the structures overlapalong the bulk of the sequences, having a common catalytic triad,corresponding to residues Asp 32, His 64, Ser 221 (numbered with respectto subtilisin BPN′ sequence, SEQ ID NO:1) and minor differences, mostlyin loops and surface exposed regions.

FIGS. 1-6 illustrate the spatial positions of a subset of the beneficialsites evaluated in this study, wherein the residues are numberedaccording to the BPN′ sequence (as shown in Table 28 above). FIG. 1shows B. subtilis (strain 168) subtilisin E (AprE) PDB entry 1SCJ(mature subtilisin region only, excluding the propeptide segment); FIG.2 shows Bacillus sp. subtilisin LG12 SprC (LG12) homology modeldescribed in WO2015038792; FIG. 3 shows B. gibsonii DSM14391 subtilisinhomology model (prepared based on the BSP-00801 B. gibsonii-cladesubtilisin structure described in WO2016205755); FIG. 4 shows B.amyloliquefaciens subtilisin BPN′ PDB entry 2ST1; FIG. 5 shows B.licheniformis subtilisin Carlsberg (AprL) PDB entry 1CSE; and FIG. 6shows B. lentus subtilisin GG36 PDB entry 1JEA. In each figure, the mainchain fold of each subtilisin is schematically represented in light grayand the following sites are depicted as black sticks: 3, 24, 40, 76, 78,79, 87, 118, 128, 129, 130, 145, 166, 182, 185, 210, 211, 217, 218, 259(BPN′ numbering). These sites are all surface exposed and are situatedin loops, outside of secondary structure motifs.

Furthermore, a subset of the sites highlighted in FIGS. 1-6 wereobserved to be distributed among the loops that together form anextended surface. In particular, sites 76, 78 and 79 (which are part ofthe same loop) are situated in spatial proximity to sites 3 and 40,which are located on distinct loops. Moreover, site 76 is also situatedin spatial proximity to site 24, which, in turn, is spatially close tosite 87 (belonging to a different loop). Site 40 resides on a loop thatis located in spatial proximity to sites 210 and 211. Thus, sites 3, 24,40, 76, 78, 79, 87, 210 and 211 (BPN′ numbering) are situated along asurface formed by a series of loops in which these sites reside. Sites128, 129 and 130 (BPN′ numbering) are in spatial proximity to site 166,as the loop containing sites 128, 129 and 130 comes close to the loopwhere site 166 is situated. Sites 182 and 185 are also located inspatial proximity to each other—these sites form part of a turn in aloop where they reside. While site 259 is located on a different loop,it appears to form part of the same surface as the loop containing sites182 and 185.

Together, the surface exposed sites 3, 9, 24, 40, 76, 78, 79, 87, 118,128, 129, 130, 145, 166, 182, 185, 210, 211, 217, 218, 248 and 259 (BPN′numbering) account for twenty-two of the twenty-four sites evaluated inthis study, and the substitutions explored were: X003T, X003V, X009E,X024Q, X040E, X069S, X076D, X078N, X079I, X087D, X118R, X124I, X128R,X128S, X129P, X130S, X145R, X166Q, X182E, X185Q, X210I, X211P, X217L,X218S, X248D, X259P. The location of these sites on the surface of themolecules, and mostly in loop regions outside of secondary structuremotifs, suggests an underlying structural commonality for theimprovements in protein stability provided by the amino acidsubstitutions evaluated in this study.

Example 13 Additional AprE & WP_082194748 Subtilisin Variants withImproved Stability in Detergent

Variants of AprE (Subtilisin E, SEQ ID NO: 8) and WP_082194748 (SEQ IDNO: 9) subtilisins containing three or four amino acid substitutions atpositions of interest to increase enzyme stability, were generated usingmethods similar to the ones described in Example 1. These variantsamples were evaluated for detergent stability (% residual activity) andcleaning performance (PI) using methods described in Example 2. Resultsfor AprE (Subtilisin E) variants are shown on Tables 30A and 30B, andresults for WP_082194748 variants are shown on Table 31.

TABLE 30A AprE subtilisin variants with improved stability in liquiddetergent at 41° C. (reported as percent residual activity, % RA)compared to AprE parent Cleaning performance, PI BMI PAS-38 AprE stainin stain in Variant Substitutions in Substitutions in PNB GSM-B SampleID AprE numbering BPN′ numbering % RA detergent detergent AprE — — 401.0 1.0 AprE-00685 S003V-N076D-S078N S003V-N076D-S078N 81 1.1 1.1AprE-00353 S003V-S078N-N218S S003V-S078N-N218S 87 1.1 1.1 AprE-00806S003V-M124I-N259P S003V-M124I-N259P 71 1.1 1.2 AprE-00696S003V-G128S-G166Q S003V-G128S-G166Q 79 1.1 1.0 AprE-00773S003V-G166Q-N218S S003V-G166Q-N218S 91 1.2 1.1 AprE-00753S003V-N218S-N259P S003V-N218S-N259P 84 1.0 1.1 AprE-00540P040E-N076D-S078N P040E-N076D-S078N 86 1.1 1.0 AprE-00635G128S-G166Q-N259P G128S-G166Q-N259P 83 1.1 1.0 AprE-00452S003V-P040E-N076D- S003V-P040E-N076D- 83 1.1 0.9 S078N S078N AprE-00850S003V-P040E-S078N- S003V-P040E-S078N- 80 1.3 1.1 M124I M124I AprE-00756S003V-P040E-M124I- S003V-P040E-M124I- 85 1.2 1.1 N218S N218S AprE-00613S003V-N076D-S078N- S003V-N076D-S078N- 100 1.2 1.0 G128S G128S AprE-00462S003V-N076D-M124I- S003V-N076D-M124I- 100 1.0 0.9 G166Q G166Q AprE-00665S003V-N076D-G128S- S003V-N076D-G128S- 100 1.2 1.0 N259P N259P AprE-00705S003V-N076D-G166Q- S003V-N076D- 91 1.1 1.1 N259P G166Q-N259P AprE-00796S003V-N076D-N218S- S003V-N076D-N218S- 96 1.1 1.1 N259P N259P AprE-00551S003V-M124I-G128S- S003V-M124I-G128S- 81 1.1 0.9 N218S N218S AprE-00617S003V-G128S-G166Q- S003V-G128S-G166Q- 99 1.3 1.0 N218S N218S AprE-00510P040E-N076D-S078N- P040E-N076D-S078N- 100 1.1 1.0 G166Q G166Q AprE-00403P040E-N076D-M124I- P040E-N076D-M124I- 93 1.2 1.0 N218S N218S AprE-00764P040E-N076D-G166Q- P040E-N076D-G166Q- 98 1.2 1.0 N218S N218S AprE-00547P040E-N076D-G166Q- P040E-N076D-G166Q- 98 1.1 1.0 N259P N259P AprE-00769N076D-S078N-M124I- N076D-S078N-M124I- 89 1.3 1.1 N218S N218S AprE-00684N076D-S078N-G128S- N076D-S078N-G128S- 94 1.2 0.9 N259P N259P AprE-00507N076D-S078N-G166Q- N076D-S078N- 97 1.0 1.0 N259P G166Q-N259P AprE-00591N076D-M124I-G128S- N076D-M124I-G128S- 100 1.1 0.8 G166Q G166Q AprE-00583N076D-M124I-G128S- N076D-M124I-G128S- 100 1.3 0.8 N259P N259P AprE-00709N076D-G128S-G166Q- N076D-G128S- 95 1.2 0.9 N218S G166Q-N218S AprE-00518S078N-G128S-G166Q- S078N-G128S-G166Q- 100 1.2 0.9 N218S N218S AprE-00589S078N-G128S-N218S- S078N-G128S-N218S- 96 1.1 1.0 N259P N259P AprE-00366M124I-G166Q-N218S- M124I-G166Q-N218S- 90 1.1 1.0 N259P N259P

TABLE 30B AprE subtilisin variants with improved stability in liquiddetergent at 42° C. (reported as percent residual activity, % RA)compared to AprE parent AprE Variant Substitutions in Substitutions inSample ID AprE numbering BPN′ numbering % RA AprE — — 27 AprE-01102S003V-S009E-P040E S003V-S009E-P040E 85 AprE-01101 S003V-S009E-A069SS003V-S009E-A069S 89 AprE-01051 S003V-S009E-N076D S003V-S009E-N076D 94AprE-01099 S003V-S009E-S078N S003V-S009E-S078N 90 AprE-01045S003V-S009E-G166Q S003V-S009E-G166Q 95 AprE-01077 S003V-S009E-N218SS003V-S009E-N218S 91 AprE-01047 S003V-S009E-N259P S003V-S009E-N259P 86AprE-01009 S003V-P040E-A069S S003V-P040E-A069S 61 AprE-01048S003V-P040E-N076D S003V-P040E-N076D 69 AprE-01915 S003V-P040E-N218SS003V-P040E-N218S 77 AprE-01039 S003V-P040E-N259P S003V-P040E-N259P 67AprE-01864 S003V-A069S-N076D S003V-A069S-N076D 54 AprE-01056S003V-A069S-S078N S003V-A069S-S078N 48 AprE-00991 S003V-A069S-G166QS003V-A069S-G166Q 75 AprE-01060 S003V-A069S-N218S S003V-A069S-N218S 70AprE-01064 S003V-A069S-N259P S003V-A069S-N259P 48 AprE-01340S003V-N076D-G166Q S003V-N076D-G166Q 100 AprE-01867 S003V-N076D-N218SS003V-N076D-N218S 82 AprE-01062 S003V-N076D-N259P S003V-N076D-N259P 84AprE-01068 S003V-S078N-N259P S003V-S078N-N259P 73 AprE-01855S003V-G166Q-N259P S003V-G166Q-N259P 68 AprE-01674 S009E-P040E-A069SS009E-P040E-A069S 73 AprE-01069 S009E-P040E-N076D S009E-P040E-N076D 94AprE-01997 S009E-P040E-S078N S009E-P040E-S078N 82 AprE-01984S009E-P040E-G166Q S009E-P040E-G166Q 88 AprE-01529 S009E-P040E-N218SS009E-P040E-N218S 97 AprE-01125 S009E-P040E-N259P S009E-P040E-N259P 88AprE-01071 S009E-A069S-N076D S009E-A069S-N076D 91 AprE-01091S009E-A069S-S078N S009E-A069S-S078N 84 AprE-01871 S009E-A069S-G166QS009E-A069S-G166Q 83 AprE-01087 S009E-A069S-N218S S009E-A069S-N218S 87AprE-01857 S009E-A069S-N259P S009E-A069S-N259P 73 AprE-01892S009E-N076D-S078N S009E-N076D-S078N 92 AprE-01093 S009E-N076D-G166QS009E-N076D-G166Q 100 AprE-01052 S009E-N076D-N218S S009E-N076D-N218S 98AprE-01860 S009E-N076D-N259P S009E-N076D-N259P 100 AprE-01095S009E-S078N-G166Q S009E-S078N-G166Q 94 AprE-01019 S009E-S078N-N218SS009E-S078N-N218S 97 AprE-01014 S009E-S078N-N259P S009E-S078N-N259P 88AprE-01029 S009E-G166Q-N218S S009E-G166Q-N218S 94 AprE-01028S009E-G166Q-N259P S009E-G166Q-N259P 97 AprE-01026 S009E-N218S-N259PS009E-N218S-N259P 94 AprE-01024 P040E-A069S-S078N P040E-A069S-S078N 44AprE-01865 P040E-A069S-G166Q P040E-A069S-G166Q 56 AprE-01823P040E-A069S-N218S P040E-A069S-N218S 61 AprE-01036 P040E-A069S-N259PP040E-A069S-N259P 48 AprE-01032 P040E-N076D-G166Q P040E-N076D-G166Q 96AprE-01824 P040E-N076D-N218S P040E-N076D-N218S 78 AprE-01031P040E-N076D-N259P P040E-N076D-N259P 81 AprE-01825 P040E-S078N-G166QP040E-S078N-G166Q 81 AprE-01030 P040E-S078N-N218S P040E-S078N-N218S 82AprE-01035 P040E-S078N-N259P P040E-S078N-N259P 59 AprE-01820P040E-G166Q-N218S P040E-G166Q-N218S 80 AprE-01831 P040E-G166Q-N259PP040E-G166Q-N259P 71 AprE-01826 P040E-N218S-N259P P040E-N218S-N259P 67AprE-01810 A069S-N076D-S078N A069S-N076D-S078N 58 AprE-01812A069S-N076D-G166Q A069S-N076D-G166Q 86 AprE-01403 A069S-N076D-N218SA069S-N076D-N218S 81 AprE-01829 A069S-N076D-N259P A069S-N076D-N259P 73AprE-01830 A069S-S078N-G166Q A069S-S078N-G166Q 69 AprE-01693A069S-S078N-N218S A069S-S078N-N218S 59 AprE-01873 A069S-S078N-N259PA069S-S078N-N259P 47 AprE-00996 A069S-G166Q-N218S A069S-G166Q-N218S 68AprE-01117 A069S-G166Q-N259P A069S-G166Q-N259P 54 AprE-01807A069S-N218S-N259P A069S-N218S-N259P 48 AprE-01805 N076D-S078N-G166QN076D-S078N-G166Q 85 AprE-01407 N076D-S078N-N218S N076D-S078N-N218S 85AprE-01118 N076D-S078N-N259P N076D-S078N-N259P 96 AprE-01802N076D-G166Q-N218S N076D-G166Q-N218S 100 AprE-01819 N076D-G166Q-N259PN076D-G166Q-N259P 92 AprE-01817 N076D-N218S-N259P N076D-N218S-N259P 87AprE-01722 S078N-G166Q-N218S S078N-G166Q-N218S 83 AprE-01816S078N-G166Q-N259P S078N-G166Q-N259P 69 AprE-01112 S078N-N218S-N259PS078N-N218S-N259P 70 AprE-01815 G166Q-N218S-N259P G166Q-N218S-N259P 67AprE-02047 S003V-P040E-A069S-G166Q S003V-P040E-A069S-G166Q 76 AprE-01188S003V-P040E-N076D-N218S S003V-P040E-N076D-N218S 81 AprE-02059S003V-A069S-G166Q-N218S S003V-A069S-G166Q-N218S 87 AprE-01547S009E-P040E-A069S-N076D S009E-P040E-A069S-N076D 84 AprE-01712S009E-P040E-A069S-N259P S009E-P040E-A069S-N259P 71 AprE-01975S009E-P040E-S078N-N259P S009E-P040E-S078N-N259P 84 AprE-01553S009E-P040E-G166Q-N218S S009E-P040E-G166Q-N218S 93 AprE-01917S009E-P040E-G166Q-N259P S009E-P040E-G166Q-N259P 88 AprE-01772S009E-P040E-N218S-N259P S009E-P040E-N218S-N259P 93 AprE-01551S009E-A069S-S078N-G166Q S009E-A069S-S078N-G166Q 88 AprE-02023S009E-S078N-N218S-N259P S009E-S078N-N218S-N259P 94 AprE-01666S009E-G166Q-N218S-N259P S009E-G166Q-N218S-N259P 94 AprE-00988P040E-A069S-N076D-S078N P040E-A069S-N076D-S078N 50 AprE-01794P040E-A069S-S078N-G166Q P040E-A069S-S078N-G166Q 75 AprE-01879P040E-A069S-S078N-N259P P040E-A069S-S078N-N259P 56 AprE-01953P040E-A069S-G166Q-N218S P040E-A069S-G166Q-N218S 83 AprE-01990N076D-S078N-G166Q-N218S N076D-S078N-G166Q-N218S 93 AprE-01979N076D-G166Q-N218S-N259P N076D-G166Q-N218S-N259P 91

TABLE 31 WP_082194748 subtilisin variants with improved stability inliquid detergent at 46° C. (reported as percent residual activity, % RA)compared to WP_082194748 parent Cleaning performance, PI PAS-38WP_082194748 Substitutions in BMI stain stain in Variant SampleWP_082194748 Substitutions in in PNB GSM-B ID numbering BPN′ numbering %RA detergent detergent WP_082194748 — — 36 1.0 1.0 WP_082194748-T003V-T078N-G166Q T003V-T078N- 93 1.2 1.5 00562 G166Q WP_082194748-T003V-T078N-S259P T003V-T078N- 70 1.4 1.3 00205 S259P WP_082194748-T003V-M124I-G128S T003V-M124I- 88 1.3 0.4 00037 G128S WP_082194748-T003V-G128S-G166Q T003V-G128S- 100 1.4 1.2 00219 G166Q WP_082194748-T003V-G128S-S259P T003V-G128S- 93 1.2 1.1 00101 S259P WP_082194748-T003V-G166Q-S259P T003V-G166Q- 98 1.3 1.3 00511 S259P WP_082194748-T078N-M124I-G166Q T078N-M124I- 80 1.4 1.3 00185 G166Q WP_082194748-T078N-G128S-G166Q T078N-G128S- 98 1.4 1.2 00433 G166Q WP_082194748-T078N-G166Q-S259P T078N-G166Q- 100 1.3 1.3 00339 S259P WP_082194748-M124I-G128S-G166Q M124I-G128S- 90 1.3 0.8 00127 G166Q WP_082194748-M124I-G166Q-S259P M124I-G166Q- 99 1.3 1.3 00218 S259P WP_082194748-T003V-T078N-M124I- T003V-T078N- 100 0.9 1.3 00547 G166Q M124I-G166QWP_082194748- T003V-T078N-G166Q- T003V-T078N- 73 1.1 1.2 00442 S259PG166Q-S259P WP_082194748- T003V-M124I-G128S- T003V-M124I- 100 1.5 0.500555 S259P G128S-S259P WP_082194748- T003V-M124I-G166Q- T003V-M124I-100 1.1 1.2 00465 S259P G166Q-S259P WP_082194748- T078N-M124I-G128S-T078N-M124I- 100 1.2 1.0 00149 S259P G128S-S259P WP_082194748-T078N-M124I-G166Q- T078N-M124I- 100 1.1 1.2 00448 S259P G166Q-S259P

Example 14 Chemgen_164A Subtilisin Variants with Improved Stability inDetergent

Variants of Chemgen_164A (Chemgen, SEQ ID NO: 10) subtilisin containingthree or four amino acid substitutions at positions of interest toincrease enzyme stability were generated using methods similar to theones described in Example 1. These variant samples were evaluated fordetergent stability (% residual activity) using methods described inExample 2. Table 32 shows the detergent stability results (% RA) forChemgen_164A variants.

TABLE 32 Chemgen_164A subtilisin variants with improved stability inliquid detergent at 51° C. (reported as percent residual activity, % RA)compared to Chemgen_164A parent Chemgen_164A Substitutions in VariantSample Chemgen_164A Substitutions in ID numbering BPN′ numbering % RAChemgen_164A — — 31 Chemgen-00801 T003V-T009E-P040E T003V-T009E-P040E 89Chemgen-01562 T003V-T009E-A069S T003V-T009E-A069S 66 Chemgen-00792T003V-T009E-N185Q T003V-T009E-N185Q 70 Chemgen-01640 T003V-P040E-N076DT003V-P040E-N076D 100 Chemgen-00793 T003V-P040E-G166Q T003V-P040E-G166Q100 Chemgen-01651 T003V-P040E-N185Q T003V-P040E-N185Q 100 Chemgen-00724T003V-P040E-D259P T003V-P040E-D259P 100 Chemgen-00816 T003V-A069S-N076DT003V-A069S-N076D 100 Chemgen-00808 T003V-A069S-T078N T003V-A069S-T078N100 Chemgen-00807 T003V-A069S-G166Q T003V-A069S-G166Q 100 Chemgen-01642T003V-A069S-N185Q T003V-A069S-N185Q 94 Chemgen-00727 T003V-A069S-N218ST003V-A069S-N218S 100 Chemgen-01658 T003V-A069S-D259P T003V-A069S-D259P100 Chemgen-00729 T003V-N076D-T078N T003V-N076D-T078N 100 Chemgen-00694T003V-N076D-G166Q T003V-N076D-G166Q 100 Chemgen-00776 T003V-N076D-N185QT003V-N076D-N185Q 100 Chemgen-00775 T003V-N076D-N218S T003V-N076D-N218S100 Chemgen-00832 T003V-N076D-D259P T003V-N076D-D259P 100 Chemgen-00774T003V-T078N-G166Q T003V-T078N-G166Q 100 Chemgen-00696 T003V-T078N-N185QT003V-T078N-N185Q 100 Chemgen-00834 T003V-T078N-D259P T003V-T078N-D259P100 Chemgen-00738 T003V-G166Q-N185Q T003V-G166Q-N185Q 100 Chemgen-00739T003V-G166Q-D259P T003V-G166Q-D259P 79 Chemgen-00785 T003V-N185Q-N218ST003V-N185Q-N218S 91 Chemgen-00698 T003V-N185Q-D259P T003V-N185Q-D259P100 Chemgen-00780 T003V-N218S-D259P T003V-N218S-D259P 100 Chemgen-01553T009E-P040E-A069S T009E-P040E-A069S 53 Chemgen-00703 T009E-P040E-N076DT009E-P040E-N076D 93 Chemgen-00683 T009E-P040E-T078N T009E-P040E-T078N81 Chemgen-00702 T009E-P040E-G166Q T009E-P040E-G166Q 78 Chemgen-00822T009E-P040E-N218S T009E-P040E-N218S 62 Chemgen-01604 T009E-P040E-D259PT009E-P040E-D259P 68 Chemgen-00684 T009E-A069S-N076D T009E-A069S-N076D79 Chemgen-00700 T009E-A069S-T078N T009E-A069S-T078N 71 Chemgen-00823T009E-A069S-G166Q T009E-A069S-G166Q 66 Chemgen-00681 T009E-A069S-N218ST009E-A069S-N218S 86 Chemgen-00829 T009E-A069S-D259P T009E-A069S-D259P46 Chemgen-00825 T009E-N076D-T078N T009E-N076D-T078N 87 Chemgen-01315T009E-N076D-G166Q T009E-N076D-G166Q 100 Chemgen-00737 T009E-N076D-N185QT009E-N076D-N185Q 78 Chemgen-00690 T009E-N076D-N218S T009E-N076D-N218S88 Chemgen-01420 T009E-N076D-D259P T009E-N076D-D259P 74 Chemgen-00826T009E-T078N-G166Q T009E-T078N-G166Q 86 Chemgen-01162 T009E-T078N-N185QT009E-T078N-N185Q 60 Chemgen-00688 T009E-T078N-N218S T009E-T078N-N218S79 Chemgen-00818 T009E-T078N-D259P T009E-T078N-D259P 80 Chemgen-00687T009E-G166Q-N218S T009E-G166Q-N218S 95 Chemgen-00686 T009E-G166Q-D259PT009E-G166Q-D259P 100 Chemgen-00705 T009E-N185Q-N218S T009E-N185Q-N218S60 Chemgen-00685 T009E-N185Q-D259P T009E-N185Q-D259P 51 Chemgen-00878P040E-A069S-N076D P040E-A069S-N076D 85 Chemgen-00876 P040E-A069S-T078NP040E-A069S-T078N 83 Chemgen-00868 P040E-A069S-G166Q P040E-A069S-G166Q63 Chemgen-01310 P040E-A069S-D259P P040E-A069S-D259P 64 Chemgen-00761P040E-N076D-T078N P040E-N076D-T078N 100 Chemgen-00642 P040E-N076D-G166QP040E-N076D-G166Q 100 Chemgen-00660 P040E-N076D-N185Q P040E-N076D-N185Q100 Chemgen-00641 P040E-N076D-N218S P040E-N076D-N218S 95 Chemgen-01465P040E-T078N-N185Q P040E-T078N-N185Q 90 Chemgen-00758 P040E-T078N-D259PP040E-T078N-D259P 100 Chemgen-00872 P040E-G166Q-N185Q P040E-G166Q-N185Q88 Chemgen-00873 P040E-G166Q-N218S P040E-G166Q-N218S 79 Chemgen-00752P040E-G166Q-D259P P040E-G166Q-D259P 84 Chemgen-00750 P040E-N185Q-N218SP040E-N185Q-N218S 66 Chemgen-00851 P040E-N185Q-D259P P040E-N185Q-D259P87 Chemgen-00845 P040E-N218S-D259P P040E-N218S-D259P 83 Chemgen-00844A069S-N076D-T078N A069S-N076D-T078N 100 Chemgen-00746 A069S-N076D-G166QA069S-N076D-G166Q 100 Chemgen-00748 A069S-N076D-N185Q A069S-N076D-N185Q79 Chemgen-01054 A069S-N076D-N218S A069S-N076D-N218S 94 Chemgen-00744A069S-N076D-D259P A069S-N076D-D259P 100 Chemgen-00861 A069S-T078N-G166QA069S-T078N-G166Q 100 Chemgen-00860 A069S-T078N-N185Q A069S-T078N-N185Q78 Chemgen-00859 A069S-T078N-N218S A069S-T078N-N218S 86 Chemgen-00756A069S-T078N-D259P A069S-T078N-D259P 78 Chemgen-00862 A069S-G166Q-N218SA069S-G166Q-N218S 100 Chemgen-00753 A069S-G166Q-D259P A069S-G166Q-D259P91 Chemgen-00659 A069S-N185Q-N218S A069S-N185Q-N218S 60 Chemgen-00863A069S-N185Q-D259P A069S-N185Q-D259P 58 Chemgen-00864 A069S-N218S-D259PA069S-N218S-D259P 79 Chemgen-00645 N076D-T078N-G166Q N076D-T078N-G166Q100 Chemgen-00865 N076D-T078N-N218S N076D-T078N-N218S 90 Chemgen-00866N076D-T078N-D259P N076D-T078N-D259P 89 Chemgen-00770 N076D-G166Q-N218SN076D-G166Q-N218S 100 Chemgen-01542 N076D-G166Q-D259P N076D-G166Q-D259P100 Chemgen-00771 N076D-N185Q-N218S N076D-N185Q-N218S 95 Chemgen-00846N076D-N218S-D259P N076D-N218S-D259P 100 Chemgen-00847 T078N-G166Q-N185QT078N-G166Q-N185Q 91 Chemgen-00763 T078N-G166Q-N218S T078N-G166Q-N218S100 Chemgen-00849 T078N-N185Q-D259P T078N-N185Q-D259P 100 Chemgen-00768T078N-N218S-D259P T078N-N218S-D259P 100 Chemgen-00765 G166Q-N185Q-N218SG166Q-N185Q-N218S 87 Chemgen-00870 G166Q-N185Q-D259P G166Q-N185Q-D259P94 Chemgen-00880 G166Q-N218S-D259P G166Q-N218S-D259P 100 Chemgen-00767N185Q-N218S-D259P N185Q-N218S-D259P 86 Chemgen-01489T003V-T009E-P040E-N185Q T003V-T009E-P040E-N185Q 65 Chemgen-01037T003V-T009E-A069S-T078N T003V-T009E-A069S-T078N 98 Chemgen-01217T003V-P040E-G166Q-D259P T003V-P040E-G166Q-D259P 100 Chemgen-01076T003V-N076D-T078N-D259P T003V-N076D-T078N-D259P 100 Chemgen-01516T003V-N185Q-N218S-D259P T003V-N185Q-N218S-D259P 100 Chemgen-01083T009E-P040E-A069S-T078N T009E-P040E-A069S-T078N 79 Chemgen-01336T009E-P040E-A069S-N185Q T009E-P040E-A069S-N185Q 61 Chemgen-00796T009E-P040E-A069S-D259P T009E-P040E-A069S-D259P 61 Chemgen-01279T009E-P040E-N076D-T078N T009E-P040E-N076D-T078N 91 Chemgen-01153T009E-P040E-T078N-N185Q T009E-P040E-T078N-N185Q 77 Chemgen-01326T009E-P040E-N185Q-N218S T009E-P040E-N185Q-N218S 68 Chemgen-01040T009E-P040E-N185Q-D259P T009E-P040E-N185Q-D259P 73 Chemgen-01521T009E-A069S-N076D-G166Q T009E-A069S-N076D-G166Q 100 Chemgen-01261T009E-A069S-N076D-N185Q T009E-A069S-N076D-N185Q 76 Chemgen-01074T009E-N076D-G166Q-N218S T009E-N076D-G166Q-N218S 98 Chemgen-01290T009E-T078N-G166Q-N185Q T009E-T078N-G166Q-N185Q 100 Chemgen-01624P040E-A069S-T078N-N218S P040E-A069S-T078N-N218S 100 Chemgen-01317P040E-A069S-G166Q-N218S P040E-A069S-G166Q-N218S 88 Chemgen-01466P040E-A069S-G166Q-D259P P040E-A069S-G166Q-D259P 89 Chemgen-01147P040E-N076D-T078N-N185Q P040E-N076D-T078N-N185Q 100 Chemgen-01000P040E-N076D-T078N-N218S P040E-N076D-T078N-N218S 100 Chemgen-01238P040E-N076D-G166Q-D259P P040E-N076D-G166Q-D259P 100 Chemgen-01578P040E-T078N-N185Q-D259P P040E-T078N-N185Q-D259P 96 Chemgen-01527P040E-T078N-N218S-D259P P040E-T078N-N218S-D259P 79 Chemgen-01548A069S-N076D-T078N-N185Q A069S-N076D-T078N-N185Q 75 Chemgen-01080A069S-N076D-T078N-D259P A069S-N076D-T078N-D259P 100 Chemgen-01510A069S-N076D-G166Q-D259P A069S-N076D-G166Q-D259P 100 Chemgen-01158A069S-T078N-G166Q-N185Q A069S-T078N-G166Q-N185Q 100 Chemgen-01278A069S-T078N-N185Q-D259P A069S-T078N-N185Q-D259P 80 Chemgen-01073N076D-T078N-G166Q-N218S N076D-T078N-G166Q-N218S 100 Chemgen-01184N076D-T078N-G166Q-D259P N076D-T078N-G166Q-D259P 100 Chemgen-01273N076D-T078N-N218S-D259P N076D-T078N-N218S-D259P 100 Chemgen-01595T078N-N185Q-N218S-D259P T078N-N185Q-N218S-D259P 100

Example 15 Bpan01744 Subtilisin Variants with Improved Stability inDetergent

Variants of Bpan01744 (SEQ ID NO: 13) subtilisin containing three orfour amino acid substitutions at positions of interest to increaseenzyme stability were generated using methods similar to the onesdescribed in Example 1. These variant samples were evaluated fordetergent stability and cleaning performance using methods described inExample 2. Tables 33A and 33B show the results for Bpan01744 variants.

TABLE 33A Bpan01744 subtilisin variants with improved stability inliquid detergent at 46° C. (reported as percent residual activity, % RA)compared to Bpan01744 parent Cleaning performance, PI Bpan01744Substitutions in Substitutions BMI stain PAS-38 stain BMI stain VariantBpan01744 in BPN′ in PNB in GSM-B in ECE-2 Sample ID numbering numbering% RA detergent detergent detergent Bpan01744 — — 11 1.0 1.0 1.0Bpan01744- S003V-A067S- S003V-A069S- 72 1.4 1.2 1.2 00169 N074D N076DBpan01744- S003V-A067S- S003V-A069S- 48 1.2 1.4 1.1 00248 S127P S129PBpan01744- S003V-A067S- S003V-A069S- 29 1.2 1.2 1.2 00150 N179Q N185QBpan01744- S003V-N074D- S003V-N076D- 81 1.3 1.3 1.0 00270 S127P S129PBpan01744- S003V-N074D- S003V-N076D- 74 1.5 1.2 1.2 00170 N179Q N185QBpan01744- S003V-S076N- S003V-S078N- 66 1.0 1.1 1.0 00059 G160Q G166QBpan01744- S003V-S127P- S003V-S129P- 40 1.2 1.1 1.3 00518 N253P N259PBpan01744- S003V-G160Q- S003V-G166Q- 85 1.1 1.0 1.0 00547 N212S N218SBpan01744- A067S-N074D- A069S-N076D- 73 1.2 1.5 1.2 00291 N179Q N185QBpan01744- A067S-G160Q- A069S-G166Q- 53 1.1 1.1 0.8 00174 N179Q N185QBpan01744- N074D-S076N- N076D-S078N- 100 1.2 1.1 0.8 00228 G160Q G166QBpan01744- N074D-S127P- N076D-S129P- 77 1.2 1.2 0.9 00478 N212S N218SBpan01744- S076N-S127P- S078N-S129P- 43 1.3 1.1 1.2 00040 N253P N259PBpan01744- S076N-N179Q- S078N-N185Q- 37 1.5 1.2 1.3 00034 N253P N259PBpan01744- S003V-A067S- S003V-A069S- 79 1.2 1.1 1.0 00224 N074D-S076NN076D-S078N Bpan01744- S003V-A067S- S003V-A069S- 73 1.5 1.5 0.9 00437N074D-N179Q N076D-N185Q Bpan01744- S003V-A067S- S003V-A069S- 75 1.2 1.21.3 00104 N074D-N253P N076D-N259P Bpan01744- S003V-A067S- S003V-A069S-51 1.2 1.1 1.1 00130 S076N-S127P S078N-S129P Bpan01744- S003V-A067S-S003V-A069S- 50 1.2 1.2 1.0 00468 S076N-N179Q S078N-N185Q Bpan01744-S003V-A067S- S003V-A069S- 67 1.1 1.1 0.8 00456 S127P-N212S S129P-N218SBpan01744- S003V-A067S- S003V-A069S- 32 1.1 0.2 1.1 00474 N179Q-N253PN185Q-N259P Bpan01744- S003V-N074D- S003V-N076D- 93 1.1 1.1 0.9 00010S127P-G160Q S129P-G166Q Bpan01744- S003V-N074D- S003V-N076D- 84 1.3 1.11.2 00155 S127P-N179Q S129P-N185Q Bpan01744- S003V-N074D- S003V-N076D-81 1.3 1.3 0.9 00470 S127P-N253P S129P-N259P Bpan01744- S003V-S076N-S003V-S078N- 78 2.2 1.4 1.4 00562 N179Q-N212S N185Q-N218S Bpan01744-S003V-S076N- S003V-S078N- 56 1.3 1.3 1.5 00164 N179Q-N253P N185Q-N259PBpan01744- S003V-G160Q- S003V-G166Q- 57 1.1 1.3 1.0 00435 N179Q-N253PN185Q-N259P Bpan01744- S003V-N179Q- S003V-N185Q- 60 1.2 1.5 1.0 00269N212S-N253P N218S-N259P Bpan01744- A067S-N074D- A069S-N076D- 84 1.3 1.20.9 00259 S076N-N212S S078N-N218S Bpan01744- A067S-N074D- A069S-N076D-76 1.2 1.1 1.1 00515 N179Q-N253P N185Q-N259P Bpan01744- A067S-S076N-A069S-S078N- 74 1.2 0.3 0.8 00272 N179Q-N212S N185Q-N218S Bpan01744-A067S-S127P- A069S-S129P- 88 0.9 1.2 0.9 00301 G160Q-N212S G166Q-N218SBpan01744- A067S-S127P- A069S-S129P- 57 1.6 1.3 1.4 00573 N179Q-N212SN185Q-N218S Bpan01744- A067S-G160Q- A069S-G166Q- 80 1.1 1.0 0.9 00035N212S-N253P N218S-N259P Bpan01744- A067S-N179Q- A069S-N185Q- 50 1.3 1.30.9 00479 N212S-N253P N218S-N259P Bpan01744- N074D-S076N- N076D-S078N-87 1.2 1.3 1.0 00415 S127P-N179Q S129P-N185Q Bpan01744- N074D-S076N-N076D-S078N- 85 1.2 1.4 1.0 00452 N179Q-N212S N185Q-N218S Bpan01744-N074D-S127P- N076D-S129P- 83 1.3 1.1 1.1 00183 N179Q-N212S N185Q-N218SBpan01744- N074D-G160Q- N076D-G166Q- 100 1.1 1.3 0.9 00261 N179Q-N253PN185Q-N259P Bpan01744- S076N-S127P- S078N-S129P- 70 1.0 1.1 1.1 00143G160Q-N253P G166Q-N259P Bpan01744- S076N-S127P- S078N-S129P- 50 1.3 1.31.1 00246 N179Q-N253P N185Q-N259P Bpan01744- S076N-G160Q- S078N-G166Q-83 1.1 1.2 1.0 00432 N212S-N253P N218S-N259P Bpan01744- S127P-G160Q-S129P-G166Q- 77 1.1 1.1 0.8 00300 N212S-N253P N218S-N259P Bpan01744-S127P-N179Q- S129P-N185Q- 53 1.2 1.3 1.1 00292 N212S-N253P N218S-N259P

TABLE 33B Bpan01744 subtilisin variants with improved stability inliquid detergent at 44° C. (reported as percent residual activity, % RA)compared to Bpan01744 parent Bpan01744 Substitutions in Variant SampleBpan01744 Substitutions in ID numbering BPN′ numbering % RA Bpan01744 —— 19 Bpan01744-01709 S003V-S009E-A067S S003V-S009E-A069S 52Bpan01744-01195 S003V-S009E-N074D S003V-S009E-N076D 91 Bpan01744-01267S003V-S009E-S076N S003V-S009E-S078N 67 Bpan01744-01140 S003V-S009E-N179QS003V-S009E-N185Q 62 Bpan01744-01141 S003V-S009E-N212S S003V-S009E-N218S86 Bpan01744-01315 S003V-S009E-N253P S003V-S009E-N259P 59Bpan01744-01142 S003V-A067S-S076N S003V-A069S-S078N 50 Bpan01744-00677S003V-A067S-N212S S003V-A069S-N218S 62 Bpan01744-01265 S003V-N074D-S076NS003V-N076D-S078N 81 Bpan01744-01585 S003V-N074D-G160Q S003V-N076D-G166Q100 Bpan01744-01252 S003V-N074D-N212S S003V-N076D-N218S 98Bpan01744-01253 S003V-S076N-N179Q S003V-S078N-N185Q 52 Bpan01744-01254S003V-S076N-N212S S003V-S078N-N218S 78 Bpan01744-01260 S003V-S076N-N253PS003V-S078N-N259P 49 Bpan01744-01274 S003V-N179Q-N212S S003V-N185Q-N218S67 Bpan01744-00685 S003V-N179Q-N253P S003V-N185Q-N259P 39Bpan01744-01275 S003V-N212S-N253P S003V-N218S-N259P 60 Bpan01744-00693S009E-A067S-N074D S009E-A069S-N076D 77 Bpan01744-00777 S009E-A067S-S076NS009E-A069S-S078N 44 Bpan01744-00898 S009E-A067S-G160Q S009E-A069S-G166Q100 Bpan01744-01231 S009E-A067S-N253P S009E-A069S-N259P 33Bpan01744-01236 S009E-N074D-S076N S009E-N076D-S078N 92 Bpan01744-01237S009E-N074D-G160Q S009E-N076D-G166Q 65 Bpan01744-01238 S009E-N074D-N179QS009E-N076D-N185Q 90 Bpan01744-01196 S009E-N074D-N212S S009E-N076D-N218S99 Bpan01744-01307 S009E-N074D-N253P S009E-N076D-N259P 73Bpan01744-01248 S009E-S076N-N179Q S009E-S078N-N185Q 59 Bpan01744-01241S009E-S076N-N212S S009E-S078N-N218S 85 Bpan01744-01242 S009E-S076N-N253PS009E-S078N-N259P 50 Bpan01744-01165 S009E-G160Q-N179Q S009E-G166Q-N185Q65 Bpan01744-01244 S009E-G160Q-N212S S009E-G166Q-N218S 99Bpan01744-00976 S009E-N179Q-N212S S009E-N185Q-N218S 78 Bpan01744-01351S009E-N179Q-N253P S009E-N185Q-N259P 31 Bpan01744-01157 S009E-N212S-N253PS009E-N218S-N259P 68 Bpan01744-00810 A067S-N074D-S076N A069S-N076D-S078N91 Bpan01744-01159 A067S-N074D-G160Q A069S-N076D-G166Q 74Bpan01744-00736 A067S-N074D-N212S A069S-N076D-N218S 85 Bpan01744-00888A067S-N074D-N253P A069S-N076D-N259P 71 Bpan01744-01154 A067S-S076N-N179QA069S-S078N-N185Q 40 Bpan01744-01162 A067S-S076N-N212S A069S-S078N-N218S70 Bpan01744-01779 A067S-S076N-N253P A069S-S078N-N259P 38Bpan01744-01885 A067S-G160Q-N212S A069S-G166Q-N218S 100 Bpan01744-00963A067S-N179Q-N212S A069S-N185Q-N218S 50 Bpan01744-01174 A067S-N212S-N253PA069S-N218S-N259P 44 Bpan01744-01182 N074D-S076N-N179Q N076D-S078N-N185Q86 Bpan01744-01173 N074D-S076N-N212S N076D-S078N-N218S 95Bpan01744-01957 N074D-S076N-N253P N076D-S078N-N259P 75 Bpan01744-01170N074D-G160Q-N212S N076D-G166Q-N218S 100 Bpan01744-01292N074D-N179Q-N212S N076D-N185Q-N218S 95 Bpan01744-01289 N074D-N179Q-N253PN076D-N185Q-N259P 76 Bpan01744-01294 S076N-G160Q-N212S S078N-G166Q-N218S86 Bpan01744-01717 S076N-N179Q-N212S S078N-N185Q-N218S 73Bpan01744-01952 S076N-N212S-N253P S078N-N218S-N259P 61 Bpan01744-00899G160Q-N179Q-N212S G166Q-N185Q-N218S 96 Bpan01744-01867 N179Q-N212S-N253PN185Q-N218S-N259P 48 Bpan01744-00749 S003V-S009E-A067S-N179QS003V-S009E-A069S-N185Q 58 Bpan01744-02012 S003V-S009E-N212S-N253PS003V-S009E-N218S-N259P 77 Bpan01744-00879 S003V-A067S-N074D-N212SS003V-A069S-N076D-N218S 94 Bpan01744-02146 S003V-A067S-N179Q-N212SS003V-A069S-N185Q-N218S 71 Bpan01744-01874 S003V-A067S-N212S-N253PS003V-A069S-N218S-N259P 59 Bpan01744-01995 S003V-N074D-N212S-N253PS003V-N076D-N218S-N259P 84 Bpan01744-01812 S003V-G160Q-N179Q-N212SS003V-G166Q-N185Q-N218S 87 Bpan01744-00832 S009E-A067S-N074D-S076NS009E-A069S-N076D-S078N 95 Bpan01744-01838 S009E-A067S-S076N-G160QS009E-A069S-S078N-G166Q 44 Bpan01744-01675 S009E-A067S-S076N-N212SS009E-A069S-S078N-N218S 87 Bpan01744-01985 S009E-A067S-G160Q-N212SS009E-A069S-G166Q-N218S 59 Bpan01744-00765 S009E-A067S-N212S-N253PS009E-A069S-N218S-N259P 67 Bpan01744-01907 S009E-N074D-S076N-G160QS009E-N076D-S078N-G166Q 77 Bpan01744-02114 S009E-N074D-S076N-N179QS009E-N076D-S078N-N185Q 90 Bpan01744-00845 S009E-N074D-N212S-N253PS009E-N076D-N218S-N259P 89 Bpan01744-01813 S009E-S076N-N179Q-N212SS009E-S078N-N185Q-N218S 87 Bpan01744-01847 S009E-S076N-N212S-N253PS009E-S078N-N218S-N259P 80 Bpan01744-00974 S009E-G160Q-N179Q-N212SS009E-G166Q-N185Q-N218S 100 Bpan01744-01036 A067S-N074D-S076N-N253PA069S-N076D-S078N-N259P 81 Bpan01744-00791 A067S-S076N-G160Q-N212SA069S-S078N-G166Q-N218S 83 Bpan01744-01856 A067S-S076N-N179Q-N253PA069S-S078N-N185Q-N259P 36 Bpan01744-00743 A067S-S076N-N212S-N253PA069S-S078N-N218S-N259P 67 Bpan01744-01873 N074D-S076N-G160Q-N179QN076D-S078N-G166Q-N185Q 100 Bpan01744-00813 N074D-S076N-G160Q-N212SN076D-S078N-G166Q-N218S 95 Bpan01744-02034 N074D-S076N-N212S-N253PN076D-S078N-N218S-N259P 86 Bpan01744-02019 N074D-G160Q-N179Q-N212SN076D-G166Q-N185Q-N218S 100 Bpan01744-01690 N074D-G160Q-N212S-N253PN076D-G166Q-N218S-N259P 86 Bpan01744-00970 N074D-N179Q-N212S-N253PN076D-N185Q-N218S-N259P 97 Bpan01744-00912 S076N-G160Q-N179Q-N212SS078N-G166Q-N185Q-N218S 95 Bpan01744-01078 S076N-G160Q-N179Q-N253PS078N-G166Q-N185Q-N259P 100

Example 16 DSM14391 Subtilisin Variants with Improved Stability inDetergent

Variants of DSM14391 (SEQ ID NO: 14) subtilisin containing three or fouramino acid substitutions at positions of interest to increase enzymestability, were generated using methods similar to the ones described inExample 1. These variant samples were evaluated for detergent stabilityand cleaning performance using methods described in Example 2. Tables34A and 34B show the results for DSM14391 variants.

TABLE 34A DSM14391 subtilisin variants with improved stability in liquiddetergent at 36° C. (reported as percent residual activity, % RA)compared to DSM14391 parent DSM14391 Variant Substitutions inSubstitutions in BMI stain in PAS-38 stain in Sample ID DSM14391numbering BPN′ numbering % RA PNB detergent GSM-B detergent DSM14391 — —11 1.0 1.0 DSM14391-00421 T003V-S039E-P212S T003V-S040E-P218S 93 1.2 1.1DSM14391-00214 T003V-G160Q-P212S T003V-G166Q-P218S 100 0.9 1.1DSM14391-00359 T003V-G160Q-N253P T003V-G166Q-N259P 75 1.0 1.2DSM14391-00272 S039E-N074D-G160Q S040E-N076D-G166Q 100 1.3 1.2DSM14391-00469 S039E-N074D-R179Q S040E-N076D-R185Q 96 1.5 1.3DSM14391-00251 S039E-S076N-D127P S040E-S078N-D129P 59 1.0 1.1DSM14391-00281 S039E-R179Q-P212S S040E-R185Q-P218S 100 1.4 1.1DSM14391-00293 S039E-R179Q-N253P S040E-R185Q-N259P 100 1.6 1.2DSM14391-00474 A067S-S076N-N253P A069S-S078N-N259P 32 1.1 1.2DSM14391-00357 A067S-D127P-P212S A069S-D129P-P218S 91 1.0 0.8DSM14391-00264 A067S-P212S-N253P A069S-P218S-N259P 100 1.1 0.9DSM14391-00473 N074D-R179Q-P212S N076D-R185Q-P218S 95 1.5 1.1DSM14391-00162 N074D-P212S-N253P N076D-P218S-N259P 100 1.0 1.1DSM14391-00170 S076N-R179Q-P212S S078N-R185Q-P218S 100 1.7 1.0DSM14391-00263 S076N-P212S-N253P S078N-P218S-N259P 100 1.0 1.0DSM14391-00169 T003V-S039E- T003V-S040E- 61 1.6 1.3 A067S-N074DA069S-N076D DSM14391-00292 T003V-S039E- T003V-S040E- 79 1.4 1.3N074D-S076N N076D-S078N DSM14391-00463 T003V-S039E- T003V-S040E- 61 1.01.1 N074D-D127P N076D-D129P DSM14391-00221 T003V-S039E- T003V-S040E- 1001.3 1.3 G160Q-R179Q G166Q-R185Q DSM14391-00457 T003V-S039E- T003V-S040E-93 1.0 1.2 G160Q-N253P G166Q-N259P DSM14391-00454 T003V-A067S-T003V-A069S- 49 1.6 1.2 R179Q-N253P R185Q-N259P DSM14391-00386T003V-N074D- T003V-N076D- 66 1.3 1.3 S076N-N253P S078N-N259PDSM14391-00328 T003V-N074D- T003V-N076D- 92 1.5 1.3 R179Q-N253PR185Q-N259P DSM14391-00179 T003V-S076N- T003V-S078N- 37 0.9 1.0D127P-N253P D129P-N259P DSM14391-00273 T003V-S076N- T003V-S078N- 100 1.11.0 P212S-N253P P218S-N259P DSM14391-00306 S039E-N074D- S040E-N076D- 1001.6 1.2 S076N-R179Q S078N-R185Q DSM14391-00178 S039E-N074D- S040E-N076D-100 1.3 1.1 P212S-N253P P218S-N259P DSM14391-00405 S039E-S076N-S040E-S078N- 100 1.2 1.1 G160Q-P212S G166Q-P218S DSM14391-00402S039E-R179Q- S040E-R185Q- 100 1.4 1.1 P212S-N253P P218S-N259PDSM14391-00226 A067S-D127P- A069S-D129P- 100 1.0 0.9 R179Q-P212SR185Q-P218S DSM14391-00267 A067S-R179Q- A069S-R185Q- 100 1.2 0.9P212S-N253P P218S-N259P DSM14391-00345 S076N-D127P- S078N-D129P- 100 1.11.0 R179Q-P212S R185Q-P218S DSM14391-00439 D127P-R179Q- D129P-R185Q- 1001.0 0.9 P212S-N253P P218S-N259P

TABLE 34B DSM14391 subtilisin variants with improved stability in liquiddetergent at 30° C. (reported as percent residual activity, % RA)compared to DSM14391 parent DSM14391 Variant Substitutions inSubstitutions in Sample ID DSM14391 numbering BPN′ numbering % RADSM14391 — — 40 DSM14391-00824 T003V-T009E-S039E T003V-T009E-S040E 98DSM14391-00996 T003V-T009E-A067S T003V-T009E-A069S 89 DSM14391-00995T003V-T009E-N074D T003V-T009E-N076D 98 DSM14391-00823 T003V-T009E-S076NT003V-T009E-S078N 100 DSM14391-00868 T003V-T009E-R179Q T003V-T009E-R185Q82 DSM14391-00822 T003V-T009E-P212S T003V-T009E-P218S 100 DSM14391-00817T003V-T009E-N253P T003V-T009E-N259P 86 DSM14391-00836 T003V-S039E-A067ST003V-S040E-A069S 77 DSM14391-00819 T003V-S039E-N074D T003V-S040E-N076D88 DSM14391-00837 T003V-S039E-S076N T003V-S040E-S078N 76 DSM14391-01004T003V-S039E-R179Q T003V-S040E-R185Q 94 DSM14391-00829 T003V-S039E-N253PT003V-S040E-N259P 70 DSM14391-00831 T003V-A067S-N074D T003V-A069S-N076D100 DSM14391-00858 T003V-A067S-R179Q T003V-A069S-R185Q 76 DSM14391-00992T003V-A067S-P212S T003V-A069S-P218S 97 DSM14391-00833 T003V-N074D-S076NT003V-N076D-S078N 86 DSM14391-01080 T003V-N074D-R179Q T003V-N076D-R185Q92 DSM14391-01084 T003V-N074D-P212S T003V-N076D-P218S 98 DSM14391-01058T003V-N074D-N253P T003V-N076D-N259P 87 DSM14391-00922 T003V-S076N-R179QT003V-S078N-R185Q 90 DSM14391-01083 T003V-S076N-P212S T003V-S078N-P218S91 DSM14391-01054 T003V-S076N-N253P T003V-S078N-N259P 68 DSM14391-00929T003V-R179Q-P212S T003V-R185Q-P218S 98 DSM14391-01078 T003V-R179Q-N253PT003V-R185Q-N259P 79 DSM14391-00919 T003V-P212S-N253P T003V-P218S-N259P97 DSM14391-00931 T009E-S039E-N074D T009E-S040E-N076D 100 DSM14391-00928T009E-S039E-S076N T009E-S040E-S078N 85 DSM14391-01025 T009E-S039E-R179QT009E-S040E-R185Q 91 DSM14391-01034 T009E-S039E-P212S T009E-S040E-P218S97 DSM14391-00899 T009E-S039E-N253P T009E-S040E-N259P 93 DSM14391-01035T009E-A067S-S076N T009E-A069S-S078N 92 DSM14391-01030 T009E-A067S-P212ST009E-A069S-P218S 88 DSM14391-01042 T009E-A067S-N253P T009E-A069S-N259P89 DSM14391-01040 T009E-N074D-S076N T009E-N076D-S078N 89 DSM14391-00908T009E-N074D-R179Q T009E-N076D-R185Q 95 DSM14391-01038 T009E-N074D-P212ST009E-N076D-P218S 95 DSM14391-01049 T009E-N074D-N253P T009E-N076D-N259P82 DSM14391-00915 T009E-S076N-R179Q T009E-S078N-R185Q 99 DSM14391-01047T009E-S076N-P212S T009E-S078N-P218S 97 DSM14391-01053 T009E-S076N-N253PT009E-S078N-N259P 98 DSM14391-01043 T009E-G160Q-P212S T009E-G166Q-P218S100 DSM14391-00911 T009E-R179Q-P212S T009E-R185Q-P218S 92 DSM14391-00912T009E-R179Q-N253P T009E-R185Q-N259P 99 DSM14391-01045 T009E-P212S-N253PT009E-P218S-N259P 98 DSM14391-01074 S039E-A067S-N074D S040E-A069S-N076D86 DSM14391-00689 S039E-A067S-R179Q S040E-A069S-R185Q 88 DSM14391-01032S039E-A067S-P212S S040E-A069S-P218S 97 DSM14391-01033 S039E-A067S-N253PS040E-A069S-N259P 88 DSM14391-01352 S039E-N074D-S076N S040E-N076D-S078N84 DSM14391-00953 S039E-N074D-P212S S040E-N076D-P218S 95 DSM14391-00686S039E-N074D-N253P S040E-N076D-N259P 91 DSM14391-01066 S039E-S076N-R179QS040E-S078N-R185Q 89 DSM14391-01065 S039E-S076N-P212S S040E-S078N-P218S97 DSM14391-00659 S039E-S076N-N253P S040E-S078N-N259P 79 DSM14391-00947S039E-G160Q-P212S S040E-G166Q-P218S 85 DSM14391-00960 S039E-P212S-N253PS040E-P218S-N259P 97 DSM14391-00945 A067S-N074D-S076N A069S-N076D-S078N81 DSM14391-01016 A067S-N074D-R179Q A069S-N076D-R185Q 91 DSM14391-01013A067S-N074D-P212S A069S-N076D-P218S 100 DSM14391-01012 A067S-N074D-N253PA069S-N076D-N259P 98 DSM14391-00883 A067S-S076N-R179Q A069S-S078N-R185Q89 DSM14391-01014 A067S-S076N-P212S A069S-S078N-P218S 96 DSM14391-01007A067S-G160Q-P212S A069S-G166Q-P218S 98 DSM14391-01105 A067S-R179Q-P212SA069S-R185Q-P218S 88 DSM14391-00882 A067S-R179Q-N253P A069S-R185Q-N259P98 DSM14391-01018 N074D-S076N-R179Q N076D-S078N-R185Q 91 DSM14391-01021N074D-S076N-P212S N076D-S078N-P218S 100 DSM14391-01019 N074D-S076N-N253PN076D-S078N-N259P 89 DSM14391-01100 N074D-G160Q-P212S N076D-G166Q-P218S74 DSM14391-01090 S076N-G160Q-P212S S078N-G166Q-P218S 76 DSM14391-01086S076N-R179Q-N253P S078N-R185Q-N259P 89 DSM14391-00893 G160Q-R179Q-P212SG166Q-R185Q-P218S 100 DSM14391-01445 G160Q-P212S-N253P G166Q-P218S-N259P100 DSM14391-00872 R179Q-P212S-N253P R185Q-P218S-N259P 100DSM14391-01556 T003V-T009E-S039E-N074D T003V-T009E-S040E-N076D 99DSM14391-01330 T003V-A067S-S076N-P212S T003V-A069S-S078N-P218S 96DSM14391-01481 T003V-G160Q-R179Q-P212S T003V-G166Q-R185Q-P218S 100DSM14391-01588 T003V-R179Q-P212S-N253P T003V-R185Q-P218S-N259P 99DSM14391-01843 T009E-S039E-A067S-P212S T009E-S040E-A069S-P218S 100DSM14391-01801 T009E-A067S-N074D-R179Q T009E-A069S-N076D-R185Q 100DSM14391-01467 T009E-N074D-S076N-R179Q T009E-N076D-S078N-R185Q 93DSM14391-01565 T009E-N074D-G160Q-P212S T009E-N076D-G166Q-P218S 97DSM14391-01293 T009E-S076N-R179Q-P212S T009E-S078N-R185Q-P218S 100DSM14391-01322 S039E-A067S-S076N-P212S S040E-A069S-S078N-P218S 100DSM14391-01634 S039E-A067S-G160Q-P212S S040E-A069S-G166Q-P218S 92DSM14391-01764 S039E-N074D-G160Q-R179Q S040E-N076D-G166Q-R185Q 100DSM14391-01881 S039E-N074D-G160Q-P212S S040E-N076D-G166Q-P218S 100DSM14391-01649 A067S-N074D-S076N-N253P A069S-N076D-S078N-N259P 88DSM14391-01617 A067S-S076N-R179Q-P212S A069S-S078N-R185Q-P218S 100DSM14391-01888 N074D-S076N-G160Q-R179Q N076D-S078N-G166Q-R185Q 81DSM14391-01490 S076N-G160Q-P212S-N253P S078N-G166Q-P218S-N259P 83DSM14391-01092 S076N-R179Q-P212S-N253P S078N-R185Q-P218S-N259P 94

Example 17 BspAI02518 Subtilisin Variants with Improved Stability inDetergent

Variants of BspAI02518 (SEQ ID NO: 16) subtilisin containing three orfour amino acid substitutions at positions of interest to increaseenzyme stability, were generated using methods similar to the onesdescribed in Example 1. These variant samples were evaluated fordetergent stability and cleaning performance using methods described inExample 2. Table 35A and 35B show the results for BspAI02518 variants.

TABLE 35A BspAI02518 subtilisin variants with improved stability inliquid detergent at 36° C. (reported as percent residual activity, % RA)compared to BspAI02518 parent Cleaning performance, PI BspAI02518Substitutions in Substitutions BMI stain PAS-38 stain BMI stain VariantBspAI02518 in BPN′ in PNB in GSM-B in ECE-2 Sample ID numberingnumbering % RA detergent detergent detergent BspAI02518 — — 12 1.0 1.01.0 BspAI02518- S003V-A067S- S003V-A069S- 29 1.1 1.9 1.2 00534 N179QN185Q BspAI02518- S003V-S076N- S003V-S078N- 38 1.1 1.2 1.0 00467 G126SG128S BspAI02518- S003V-N179Q- S003V-N185Q- 40 0.8 1.0 0.8 00539 N253PN259P BspAI02518- A067S-N074D- A069S-N076D- 57 1.6 5.4 1.9 00442 G126SG128S BspAI02518- A067S-N074D- A069S-N076D- 73 1.2 1.2 0.8 00870 N212SN218S BspAI02518- A067S-S076N- A069S-S078N- 23 1.1 1.3 0.9 00868 M122IM124I BspAI02518- N074D-S076N- N076D-S078N- 77 1.1 2.1 1.5 00999 N179QN185Q BspAI02518- N074D-S076N- N076D-S078N- 86 1.0 1.0 0.9 00507 N212SN218S BspAI02518- N074D-G126S- N076D-G128S- 69 1.5 2.8 1.5 00939 S160QS166Q BspAI02518- M122I-G126S- M124I-G128S- 21 1.2 1.1 0.6 00708 N179QN185Q BspAI02518- G126S-S160Q- G128S-S166Q- 40 1.3 1.8 1.0 00607 N179QN185Q BspAI02518- S003V-A067S- S003V-A069S- 62 1.5 4.8 1.8 01017N074D-G126S N076D-G128S BspAI02518- S003V-A067S- S003V-A069S- 32 1.1 1.71.2 00435 S076N-G126S S078N-G128S BspAI02518- S003V-A067S- S003V-A069S-60 0.9 1.9 1.4 00768 S076N-S160Q S078N-S166Q BspAI02518- S003V-A067S-S003V-A069S- 56 1.0 1.0 1.0 00518 M122I-N212S M124I-N218S BspAI02518-S003V-A067S- S003V-A069S- 47 1.4 2.3 1.8 00555 G126S-S160Q G128S-S166QBspAI02518- S003V-A067S- S003V-A069S- 18 1.3 1.0 0.8 00887 G126S-N253PG128S-N259P BspAI02518- S003V-N074D- S003V-N076D- 88 1.2 1.6 1.0 00658S160Q-N179Q S166Q-N185Q BspAI02518- S003V-S076N- S003V-S078N- 70 1.0 1.00.8 01005 M122I-S160Q M124I-S166Q BspAI02518- S003V-S076N- S003V-S078N-50 1.0 1.1 1.0 00556 G126S-N179Q G128S-N185Q BspAI02518- S003V-S076N-S003V-S078N- 75 1.0 1.0 0.9 00509 G126S-N212S G128S-N218S BspAI02518-S003V-M122I- S003V-M124I- 60 0.9 1.2 0.8 00648 S160Q-N253P S166Q-N259PBspAI02518- S003V-M122I- S003V-M124I- 36 1.1 1.2 0.8 00840 N179Q-N253PN185Q-N259P BspAI02518- S003V-G126S- S003V-G128S- 60 1.2 1.1 0.8 00877N179Q-N212S N185Q-N218S BspAI02518- S003V-G126S- S003V-G128S- 60 1.0 1.00.7 00567 N212S-N253P N218S-N259P BspAI02518- S003V-S160Q- S003V-S166Q-83 0.8 1.0 0.8 00615 N212S-N253P N218S-N259P BspAI02518- A067S-N074D-A069S-N076D- 66 1.7 10.9 2.8 00738 S076N-G126S S078N-G128S BspAI02518-A067S-N074D- A069S-N076D- 70 1.5 2.6 0.8 00888 M122I-G126S M124I-G128SBspAI02518- A067S-N074D- A069S-N076D- 89 1.2 2.4 1.8 00581 S160Q-N212SS166Q-N218S BspAI02518- A067S-N074D- A069S-N076D- 57 1.4 2.2 1.4 00919N179Q-N253P N185Q-N259P BspAI02518- A067S-N074D- A069S-N076D- 76 1.3 1.31.1 00530 N212S-N253P N218S-N259P BspAI02518- A067S-S076N- A069S-S078N-57 0.9 1.0 0.9 00745 G126S-N212S G128S-N218S BspAI02518- A067S-S076N-A069S-S078N- 34 0.9 1.3 1.1 00978 N179Q-N253P N185Q-N259P BspAI02518-A067S-M122I- A069S-M124I- 39 1.1 1.2 0.3 00508 G126S-N179Q G128S-N185QBspAI02518- A067S-M122I- A069S-M124I- 36 1.2 1.1 0.7 00921 G126S-N212SG128S-N218S BspAI02518- A067S-G126S- A069S-G128S- 71 1.4 1.6 1.2 00699S160Q-N212S S166Q-N218S BspAI02518- A067S-G126S- A069S-G128S- 43 1.0 0.80.7 01013 N212S-N253P N218S-N259P BspAI02518- N074D-S160Q- N076D-S166Q-78 0.9 1.2 0.7 00815 N179Q-N253P N185Q-N259P BspAI02518- S076N-M122I-S078N-M124I- 56 1.1 1.1 0.5 00867 G126S-N212S G128S-N218S BspAI02518-S076N-N179Q- S078N-N185Q- 75 1.1 1.2 1.0 00702 N212S-N253P N218S-N259PBspAI02518- M122I-G126S- M124I-G128S- 43 1.0 1.1 0.4 00866 S160Q-N253PS166Q-N259P BspAI02518- M122I-S160Q- M124I-S166Q- 78 1.0 1.0 0.8 00885N212S-N253P N218S-N259P BspAI02518- G126S-S160Q- G128S-S166Q- 38 1.2 1.10.9 00504 N179Q-N253P N185Q-N259P

TABLE 35B BspAI02518 subtilisin variants with improved stability inliquid detergent at 30° C. (reported as percent residual activity, % RA)compared to BspAI02518 parent BspAI02518 Variant Substitutions inSubstitutions in Sample ID BspAI02518 numbering BPN′ numbering % RABspAI02518 — — 32 BspAI02518-01092 S003V-S009E-A067S S003V-S009E-A069S68 BspAI02518-01095 S003V-S009E-N074D S003V-S009E-N076D 93BspAI02518-01270 S003V-S009E-S076N S003V-S009E-S078N 74 BspAI02518-01096S003V-S009E-S160Q S003V-S009E-S166Q 87 BspAI02518-01276S003V-S009E-N179Q S003V-S009E-N185Q 75 BspAI02518-01097S003V-S009E-N212S S003V-S009E-N218S 90 BspAI02518-01282S003V-S009E-N253P S003V-S009E-N259P 100 BspAI02518-01085S003V-A067S-N074D S003V-A069S-N076D 84 BspAI02518-01086S003V-A067S-S076N S003V-A069S-S078N 61 BspAI02518-01087S003V-A067S-N212S S003V-A069S-N218S 71 BspAI02518-01088S003V-N074D-S076N S003V-N076D-S078N 83 BspAI02518-01250S003V-N074D-S160Q S003V-N076D-S166Q 88 BspAI02518-01084S003V-N074D-N179Q S003V-N076D-N185Q 89 BspAI02518-01220S003V-N074D-N212S S003V-N076D-N218S 83 BspAI02518-01230S003V-N074D-N253P S003V-N076D-N259P 73 BspAI02518-01222S003V-S076N-S160Q S003V-S078N-S166Q 80 BspAI02518-01895S003V-S076N-N179Q S003V-S078N-N185Q 68 BspAI02518-01231S003V-S076N-N212S S003V-S078N-N218S 83 BspAI02518-01992S003V-S076N-N253P S003V-S078N-N259P 65 BspAI02518-01110S003V-S160Q-N179Q S003V-S166Q-N185Q 70 BspAI02518-02118S003V-S160Q-N253P S003V-S166Q-N259P 76 BspAI02518-01099S003V-N179Q-N212S S003V-N185Q-N218S 83 BspAI02518-01960S003V-N212S-N253P S003V-N218S-N259P 74 BspAI02518-01238S009E-A067S-N074D S009E-A069S-N076D 81 BspAI02518-01102S009E-A067S-N179Q S009E-A069S-N185Q 70 BspAI02518-01165S009E-A067S-N212S S009E-A069S-N218S 83 BspAI02518-01105S009E-N074D-S076N S009E-N076D-S078N 89 BspAI02518-01235S009E-N074D-S160Q S009E-N076D-S166Q 94 BspAI02518-01153S009E-N074D-N179Q S009E-N076D-N185Q 87 BspAI02518-02121S009E-N074D-N212S S009E-N076D-N218S 99 BspAI02518-01107S009E-N074D-N253P S009E-N076D-N259P 80 BspAI02518-02083S009E-S076N-S160Q S009E-S078N-S166Q 80 BspAI02518-01268S009E-S076N-N179Q S009E-S078N-N185Q 67 BspAI02518-01140S009E-S076N-N212S S009E-S078N-N218S 88 BspAI02518-01142S009E-S076N-N253P S009E-S078N-N259P 72 BspAI02518-01167S009E-S160Q-N179Q S009E-S166Q-N185Q 81 BspAI02518-01138S009E-S160Q-N212S S009E-S166Q-N218S 90 BspAI02518-01226S009E-S160Q-N253P S009E-S166Q-N259P 82 BspAI02518-01227S009E-N179Q-N212S S009E-N185Q-N218S 80 BspAI02518-01148S009E-N179Q-N253P S009E-N185Q-N259P 56 BspAI02518-01251S009E-N212S-N253P S009E-N218S-N259P 87 BspAI02518-01243A067S-N074D-S076N A069S-N076D-S078N 86 BspAI02518-01245A067S-N074D-S160Q A069S-N076D-S166Q 86 BspAI02518-01139A067S-N074D-N179Q A069S-N076D-N185Q 75 BspAI02518-01219A067S-N074D-N253P A069S-N076D-N259P 70 BspAI02518-01205A067S-S076N-S160Q A069S-S078N-S166Q 74 BspAI02518-01207A067S-S076N-N212S A069S-S078N-N218S 80 BspAI02518-01166A067S-S160Q-N179Q A069S-S166Q-N185Q 66 BspAI02518-01201A067S-S160Q-N212S A069S-S166Q-N218S 84 BspAI02518-01151A067S-S160Q-N253P A069S-S166Q-N259P 64 BspAI02518-01215A067S-N179Q-N212S A069S-N185Q-N218S 73 BspAI02518-01202A067S-N212S-N253P A069S-N218S-N259P 69 BspAI02518-01199N074D-S076N-S160Q N076D-S078N-S166Q 93 BspAI02518-01218N074D-S076N-N253P N076D-S078N-N259P 76 BspAI02518-01210N074D-S160Q-N179Q N076D-S166Q-N185Q 85 BspAI02518-01211N074D-S160Q-N212S N076D-S166Q-N218S 96 BspAI02518-01212N074D-S160Q-N253P N076D-S166Q-N259P 91 BspAI02518-01124N074D-N179Q-N212S N076D-N185Q-N218S 92 BspAI02518-01132N074D-N179Q-N253P N076D-N185Q-N259P 80 BspAI02518-01122N074D-N212S-N253P N076D-N218S-N259P 88 BspAI02518-02142S076N-S160Q-N179Q S078N-S166Q-N185Q 89 BspAI02518-01128S076N-S160Q-N212S S078N-S166Q-N218S 89 BspAI02518-01119S076N-S160Q-N253P S078N-S166Q-N259P 67 BspAI02518-01114S076N-N179Q-N212S S078N-N185Q-N218S 83 BspAI02518-01263S076N-N179Q-N253P S078N-N185Q-N259P 62 BspAI02518-01115S076N-N212S-N253P S078N-N218S-N259P 79 BspAI02518-01265S160Q-N179Q-N212S S166Q-N185Q-N218S 86 BspAI02518-01117S160Q-N179Q-N253P S166Q-N185Q-N259P 65 BspAI02518-01116S160Q-N212S-N253P S166Q-N218S-N259P 84 BspAI02518-01621S003V-S009E-N074D-S160Q S003V-S009E-N076D-S166Q 100 BspAI02518-02172S003V-A067S-S076N-N253P S003V-A069S-S078N-N259P 64 BspAI02518-02095S003V-A067S-S160Q-N212S S003V-A069S-S166Q-N218S 93 BspAI02518-01687S003V-N074D-S076N-S160Q S003V-N076D-S078N-S166Q 96 BspAI02518-01786S003V-N074D-S076N-N253P S003V-N076D-S078N-N259P 82 BspAI02518-01818S003V-N074D-S160Q-N253P S003V-N076D-S166Q-N259P 95 BspAI02518-01782S003V-S160Q-N179Q-N253P S003V-S166Q-N185Q-N259P 82 BspAI02518-02090S009E-A067S-N074D-S160Q S009E-A069S-N076D-S166Q 85 BspAI02518-01666S009E-A067S-N074D-N212S S009E-A069S-N076D-N218S 87 BspAI02518-01743S009E-A067S-N074D-N253P S009E-A069S-N076D-N259P 86 BspAI02518-01859S009E-A067S-S076N-S160Q S009E-A069S-S078N-S166Q 84 BspAI02518-01646S009E-A067S-S076N-N212S S009E-A069S-S078N-N218S 81 BspAI02518-01924S009E-A067S-S160Q-N253P S009E-A069S-S166Q-N259P 88 BspAI02518-01696S009E-N074D-S076N-N253P S009E-N076D-S078N-N259P 92 BspAI02518-02000S009E-N074D-S160Q-N179Q S009E-N076D-S166Q-N185Q 89 BspAI02518-01753S009E-N074D-S160Q-N253P S009E-N076D-S166Q-N259P 94 BspAI02518-01299S009E-N074D-N179Q-N212S S009E-N076D-N185Q-N218S 93 BspAI02518-01620S009E-N074D-N179Q-N253P S009E-N076D-N185Q-N259P 75 BspAI02518-01959S009E-S076N-S160Q-N212S S009E-S078N-S166Q-N218S 96 BspAI02518-01703S009E-S076N-N179Q-N253P S009E-S078N-N185Q-N259P 77 BspAI02518-01628S009E-S076N-N212S-N253P S009E-S078N-N218S-N259P 94 BspAI02518-01708A067S-N074D-S076N-N212S A069S-N076D-S078N-N218S 97 BspAI02518-01144A067S-N074D-S160Q-N179Q A069S-N076D-S166Q-N185Q 93 BspAI02518-01638A067S-N074D-N179Q-N212S A069S-N076D-N185Q-N218S 85 BspAI02518-01256A067S-S076N-S160Q-N212S A069S-S078N-S166Q-N218S 94 BspAI02518-01627A067S-S076N-N179Q-N212S A069S-S078N-N185Q-N218S 86 BspAI02518-01693A067S-S076N-N212S-N253P A069S-S078N-N218S-N259P 87 BspAI02518-01677A067S-S160Q-N179Q-N212S A069S-S166Q-N185Q-N218S 81 BspAI02518-01730A067S-S160Q-N179Q-N253P A069S-S166Q-N185Q-N259P 60 BspAI02518-01887N074D-S076N-S160Q-N212S N076D-S078N-S166Q-N218S 100 BspAI02518-01778N074D-S076N-N179Q-N212S N076D-S078N-N185Q-N218S 98 BspAI02518-01581N074D-S076N-N179Q-N253P N076D-S078N-N185Q-N259P 76 BspAI02518-01720N074D-S076N-N212S-N253P N076D-S078N-N218S-N259P 96 BspAI02518-01842N074D-S160Q-N179Q-N212S N076D-S166Q-N185Q-N218S 100 BspAI02518-02079N074D-S160Q-N212S-N253P N076D-S166Q-N218S-N259P 86 BspAI02518-02016N074D-N179Q-N212S-N253P N076D-N185Q-N218S-N259P 93 BspAI02518-01792S076N-S160Q-N179Q-N212S S078N-S166Q-N185Q-N218S 93 BspAI02518-02157S076N-S160Q-N179Q-N253P S078N-S166Q-N185Q-N259P 93 BspAI02518-01716S160Q-N179Q-N212S-N253P S166Q-N185Q-N218S-N259P 88

Example 18 Bad02409 Subtilisin Variants with Improved Stability inDetergent

Variants of Bad02409 (SEQ ID NO: 18) subtilisin containing three or fouramino acid substitutions at positions of interest to increase enzymestability, were generated using methods similar to the ones described inExample 1. These variant samples were evaluated for detergent stabilityand cleaning performance using methods described in Example 2. Table 36shows the results for Bad02409 variants.

TABLE 36 Bad02409 subtilisin variants with improved stability in liquiddetergent at 67° C. (reported as percent residual activity, % RA)compared to Bad02409 parent Cleaning performance, PI BMI stain PAS-38stain Bad02409 Variant Substitutions in Substitutions in in PNB in GSM-BSample ID Bad02409 numbering BPN′ numbering % RA detergent detergentBad02409 — — 21 1.0 1.0 Bad02409-00464 T003V-A071S-G169QT003V-A069S-G166Q 47 1.4 1.1 Bad02409-00516 T003V-N078D-D262PT003V-N076D-D259P 76 1.1 0.9 Bad02409-00380 T003V-S080N-N188QT003V-S078N-N185Q 51 1.0 1.2 Bad02409-00327 T003V-S131P-N188QT003V-S129P-N185Q 40 1.0 1.2 Bad02409-00323 T003V-G169Q-D262PT003V-G166Q-D259P 43 1.2 1.1 Bad02409-00167 T003V-N188Q-D262PT003V-N185Q-D259P 45 0.9 1.1 Bad02409-00548 A071S-N078D-G169QA069S-N076D-G166Q 73 1.1 0.9 Bad02409-00344 N078D-G169Q-N188QN076D-G166Q-N185Q 64 1.4 1.1 Bad02409-00417 T003V-A071S- T003V-A069S- 551.0 1.0 S080N-S131P S078N-S129P Bad02409-00014 T003V-N078D- T003V-N076D-55 1.0 1.2 N188Q-D262P N185Q-D259P Bad02409-00195 T003V-S080N-T003V-S078N- 52 1.4 1.2 S131P-N188Q S129P-N185Q Bad02409-00098T003V-S080N- T003V-S078N- 77 1.3 1.1 G169Q-D262P G166Q-D259PBad02409-00455 T003V-G169Q- T003V-G166Q- 46 1.2 1.2 N188Q-D262PN185Q-D259P Bad02409-00209 A071S-N078D- A069S-N076D- 82 0.9 1.1S131P-D262P S129P-D259P Bad02409-00465 A071S-S080N- A069S-S078N- 47 1.31.0 S131P-N188Q S129P-N185Q Bad02409-00130 A071S-S131P- A069S-S129P- 381.5 1.0 G169Q-N188Q G166Q-N185Q Bad02409-00349 N078D-S080N- N076D-S078N-71 0.9 1.0 S131P-N188Q S129P-N185Q Bad02409-00469 N078D-S131P-N076D-S129P- 80 1.0 1.0 G169Q-D262P G166Q-D259P Bad02409-00444N078D-G169Q- N076D-G166Q- 66 1.3 1.2 N188Q-D262P N185Q-D259P

Example 19 Bba02069 Subtilisin Variants with Improved Stability inDetergent

Variants of Bba02069 (SEQ ID NO: 19) subtilisin containing three or fouramino acid substitutions at positions of interest to increase enzymestability, were generated using methods similar to the ones described inExample 1. These variant samples were evaluated for detergent stabilityand cleaning performance using methods described in Example 2. Table 37Aand 37B show the results for Bba02069 variants.

TABLE 37A Bba02069 subtilisin variants with improved stability in liquiddetergent at 40° C. (reported as percent residual activity, % RA)compared to Bba02069 parent Cleaning performance, PI Bba02069Substitutions in Substitutions BMI stain PAS-38 stain BMI stain VariantBba02069 in BPN′ in PNB in GSM-B in ECE-2 Sample ID numbering numbering% RA detergent detergent detergent Bba02069 — — 30 1.0 1.0 1.0 Bba02069-Q003V-P040E- Q003V-P040E- 85 0.9 1.2 0.9 00013 G167Q G166Q Bba02069-Q003V-G167Q- Q003V-G166Q- 84 0.8 1.0 1.2 00471 S260P S259P Bba02069-A069S-S129P- A069S-S129P- 68 0.9 1.0 0.9 00211 G167Q G166Q Bba02069-A069S-S129P- A069S-S129P- 59 1.0 0.5 0.7 00305 V186Q V185Q Bba02069-G128S-S129P- G128S-S129P- 54 0.9 1.0 0.9 00443 N219S N218S Bba02069-G128S-V186Q- G128S-V185Q- 74 0.7 1.1 0.9 00510 N219S N218S Bba02069-Q003V-A069S- Q003V-A069S- 84 0.7 1.0 1.0 00170 S129P-S260P S129P-S259PBba02069- Q003V-M124I- Q003V-M124I- 100 0.6 1.3 0.7 00558 G128S-G167QG128S-G166Q Bba02069- Q003V-G128S- Q003V-G128S- 73 0.8 1.2 0.9 00196S129P-V186Q S129P-V185Q Bba02069- P040E-A069S- P040E-A069S- 82 1.1 1.00.9 00183 S129P-N219S S129P-N218S Bba02069- P040E-M124I- P040E-M124I- 870.9 1.2 0.6 00248 N219S-S260P N218S-S259P Bba02069- A069S-N076D-A069S-N076D- 96 1.0 1.0 1.1 00543 S129P-G167Q S129P-G166Q Bba02069-A069S-M124I- A069S-M124I- 77 0.9 1.3 0.7 00437 S129P-S260P S129P-S259PBba02069- A069S-M124I- A069S-M124I- 83 0.6 1.2 0.5 00469 V186Q-N219SV185Q-N218S Bba02069- G128S-G167Q- G128S-G166Q- 76 0.9 0.9 1.0 00022V186Q-N219S V185Q-N218S Bba02069- S129P-G167Q- S129P-G166Q- 62 0.8 1.21.1 00484 V186Q-S260P V185Q-S259P

TABLE 37B Bba02069 subtilisin variants with improved stability in liquiddetergent at 39° C. (reported as percent residual activity, % RA)compared to Bba02069 parent Bba02069 Variant Substitutions inSubstitutions in Sample ID Bba02069 numbering BPN′ numbering % RABba02069 — — 23 Bba02069-00812 Q003V-T009E-P040E Q003V-T009E-P040E 88Bba02069-00811 Q003V-T009E-A069S Q003V-T009E-A069S 77 Bba02069-00809Q003V-T009E-N076D Q003V-T009E-N076D 100 Bba02069-00744 Q003V-T009E-G167QQ003V-T009E-G166Q 95 Bba02069-00808 Q003V-T009E-V186Q Q003V-T009E-V185Q83 Bba02069-00829 Q003V-T009E-N219S Q003V-T009E-N218S 98 Bba02069-00843Q003V-T009E-S260P Q003V-T009E-S259P 86 Bba02069-00747 Q003V-P040E-A069SQ003V-P040E-A069S 89 Bba02069-00833 Q003V-P040E-N076D Q003V-P040E-N076D88 Bba02069-00664 Q003V-P040E-V186Q Q003V-P040E-V185Q 74 Bba02069-00781Q003V-P040E-N219S Q003V-P040E-N218S 74 Bba02069-00834 Q003V-P040E-S260PQ003V-P040E-S259P 84 Bba02069-00779 Q003V-A069S-N076D Q003V-A069S-N076D78 Bba02069-00778 Q003V-A069S-G167Q Q003V-A069S-G166Q 95 Bba02069-00679Q003V-A069S-N219S Q003V-A069S-N218S 81 Bba02069-00776 Q003V-A069S-S260PQ003V-A069S-S259P 81 Bba02069-00836 Q003V-N076D-G167Q Q003V-N076D-G166Q89 Bba02069-00827 Q003V-N076D-V186Q Q003V-N076D-V185Q 86 Bba02069-00825Q003V-N076D-N219S Q003V-N076D-N218S 91 Bba02069-00842 Q003V-N076D-S260PQ003V-N076D-S259P 91 Bba02069-00760 Q003V-G167Q-V186Q Q003V-G166Q-V185Q82 Bba02069-00840 Q003V-G167Q-N219S Q003V-G166Q-N218S 98 Bba02069-00838Q003V-V186Q-S260P Q003V-V185Q-S259P 73 Bba02069-00764 Q003V-N219S-S260PQ003V-N218S-S259P 88 Bba02069-00846 T009E-P040E-A069S T009E-P040E-A069S64 Bba02069-00886 T009E-P040E-N076D T009E-P040E-N076D 97 Bba02069-00847T009E-P040E-G167Q T009E-P040E-G166Q 92 Bba02069-01933 T009E-P040E-V186QT009E-P040E-V185Q 70 Bba02069-01674 T009E-P040E-N219S T009E-P040E-N218S94 Bba02069-00763 T009E-P040E-S260P T009E-P040E-S259P 81 Bba02069-00848T009E-A069S-N076D T009E-A069S-N076D 90 Bba02069-00849 T009E-A069S-G167QT009E-A069S-G166Q 94 Bba02069-00791 T009E-A069S-V186Q T009E-A069S-V185Q67 Bba02069-00722 T009E-A069S-N219S T009E-A069S-N218S 87 Bba02069-00795T009E-A069S-S260P T009E-A069S-S259P 88 Bba02069-00796 T009E-N076D-G167QT009E-N076D-G166Q 94 Bba02069-00725 T009E-N076D-V186Q T009E-N076D-V185Q93 Bba02069-01905 T009E-N076D-N219S T009E-N076D-N218S 99 Bba02069-00793T009E-N076D-S260P T009E-N076D-S259P 98 Bba02069-00794 T009E-G167Q-V186QT009E-G166Q-V185Q 83 Bba02069-00797 T009E-G167Q-N219S T009E-G166Q-N218S91 Bba02069-00715 T009E-G167Q-S260P T009E-G166Q-S259P 84 Bba02069-00799T009E-V186Q-N219S T009E-V185Q-N218S 88 Bba02069-00718 T009E-V186Q-S260PT009E-V185Q-S259P 78 Bba02069-00801 T009E-N219S-S260P T009E-N218S-S259P87 Bba02069-00720 P040E-A069S-N076D P040E-A069S-N076D 100 Bba02069-00802P040E-A069S-G167Q P040E-A069S-G166Q 65 Bba02069-01826 P040E-A069S-V186QP040E-A069S-V185Q 48 Bba02069-00882 P040E-A069S-N219S P040E-A069S-N218S70 Bba02069-00730 P040E-A069S-S260P P040E-A069S-S259P 66 Bba02069-00693P040E-N076D-G167Q P040E-N076D-G166Q 98 Bba02069-00729 P040E-N076D-V186QP040E-N076D-V185Q 79 Bba02069-00695 P040E-N076D-N219S P040E-N076D-N218S84 Bba02069-00696 P040E-N076D-S260P P040E-N076D-S259P 94 Bba02069-00692P040E-G167Q-V186Q P040E-G166Q-V185Q 52 Bba02069-00691 P040E-G167Q-N219SP040E-G166Q-N218S 87 Bba02069-00705 P040E-G167Q-S260P P040E-G166Q-S259P69 Bba02069-00706 P040E-V186Q-N219S P040E-V185Q-N218S 76 Bba02069-00686P040E-V186Q-S260P P040E-V185Q-S259P 54 Bba02069-00685 P040E-N219S-S260PP040E-N218S-S259P 77 Bba02069-00708 A069S-N076D-G167Q A069S-N076D-G166Q92 Bba02069-00883 A069S-N076D-V186Q A069S-N076D-V185Q 75 Bba02069-00684A069S-N076D-N219S A069S-N076D-N218S 88 Bba02069-00683 A069S-N076D-S260PA069S-N076D-S259P 92 Bba02069-00703 A069S-G167Q-V186Q A069S-G166Q-V185Q51 Bba02069-01832 A069S-G167Q-N219S A069S-G166Q-N218S 85 Bba02069-00704A069S-G167Q-S260P A069S-G166Q-S259P 73 Bba02069-01679 A069S-V186Q-N219SA069S-V185Q-N218S 65 Bba02069-00930 A069S-V186Q-S260P A069S-V185Q-S259P52 Bba02069-00700 A069S-N219S-S260P A069S-N218S-S259P 72 Bba02069-00699N076D-G167Q-V186Q N076D-G166Q-V185Q 95 Bba02069-00698 N076D-G167Q-N219SN076D-G166Q-N218S 100 Bba02069-01319 N076D-G167Q-S260P N076D-G166Q-S259P95 Bba02069-01333 N076D-V186Q-N219S N076D-V185Q-N218S 94 Bba02069-01321N076D-V186Q-S260P N076D-V185Q-S259P 89 Bba02069-01323 N076D-N219S-S260PN076D-N218S-S259P 97 Bba02069-01324 G167Q-V186Q-N219S G166Q-V185Q-N218S64 Bba02069-01335 G167Q-V186Q-S260P G166Q-V185Q-S259P 52 Bba02069-01328G167Q-N219S-S260P G166Q-N218S-S259P 73 Bba02069-01329 V186Q-N219S-S260PV185Q-N218S-S259P 60 Bba02069-01318 Q003V-T009E-P040E-G167QQ003V-T009E-P040E-G166Q 97 Bba02069-01136 Q003V-T009E-P040E-V186QQ003V-T009E-P040E-V185Q 82 Bba02069-01264 Q003V-T009E-N076D-N219SQ003V-T009E-N076D-N218S 82 Bba02069-01585 Q003V-T009E-G167Q-V186QQ003V-T009E-G166Q-V185Q 95 Bba02069-01764 Q003V-P040E-N076D-V186QQ003V-P040E-N076D-V185Q 73 Bba02069-01124 T009E-P040E-A069S-V186QT009E-P040E-A069S-V185Q 80 Bba02069-01219 T009E-P040E-A069S-N219ST009E-P040E-A069S-N218S 100 Bba02069-01040 T009E-P040E-N076D-V186QT009E-P040E-N076D-V185Q 99 Bba02069-01182 T009E-A069S-N076D-N219ST009E-A069S-N076D-N218S 98 Bba02069-01203 T009E-A069S-G167Q-V186QT009E-A069S-G166Q-V185Q 83 Bba02069-01007 T009E-A069S-G167Q-N219ST009E-A069S-G166Q-N218S 100 Bba02069-00924 T009E-A069S-V186Q-N219ST009E-A069S-V185Q-N218S 82 Bba02069-00904 T009E-N076D-V186Q-S260PT009E-N076D-V185Q-S259P 98 Bba02069-00908 T009E-V186Q-N219S-S260PT009E-V185Q-N218S-S259P 83 Bba02069-01165 P040E-A069S-N076D-V186QP040E-A069S-N076D-V185Q 89 Bba02069-01900 P040E-A069S-G167Q-N219SP040E-A069S-G166Q-N218S 94 Bba02069-01768 P040E-A069S-V186Q-N219SP040E-A069S-V185Q-N218S 67 Bba02069-01072 P040E-A069S-V186Q-S260PP040E-A069S-V185Q-S259P 72 Bba02069-01470 P040E-A069S-N219S-S260PP040E-A069S-N218S-S259P 82 Bba02069-01003 P040E-N076D-G167Q-V186QP040E-N076D-G166Q-V185Q 94 Bba02069-00893 P040E-N076D-V186Q-N219SP040E-N076D-V185Q-N218S 86 Bba02069-00996 P040E-N076D-V186Q-S260PP040E-N076D-V185Q-S259P 92 Bba02069-01478 P040E-G167Q-V186Q-N219SP040E-G166Q-V185Q-N218S 79 Bba02069-01856 P040E-V186Q-N219S-S260PP040E-V185Q-N218S-S259P 78 Bba02069-00954 A069S-N076D-G167Q-V186QA069S-N076D-G166Q-V185Q 95 Bba02069-01024 A069S-N076D-G167Q-N219SA069S-N076D-G166Q-N218S 96 Bba02069-01011 A069S-N076D-G167Q-S260PA069S-N076D-G166Q-S259P 97 Bba02069-01803 A069S-N076D-V186Q-N219SA069S-N076D-V185Q-N218S 94 Bba02069-01919 A069S-N076D-N219S-S260PA069S-N076D-N218S-S259P 93 Bba02069-01842 A069S-G167Q-V186Q-N219SA069S-G166Q-V185Q-N218S 62 Bba02069-01958 N076D-G167Q-V186Q-S260PN076D-G166Q-V185Q-S259P 93 Bba02069-01312 N076D-G167Q-N219S-S260PN076D-G166Q-N218S-S259P 99 Bba02069-01570 G167Q-V186Q-N219S-S260PG166Q-V185Q-N218S-S259P 68

Example 20 BspZ00258 Subtilisin Variants with Improved Stability inDetergent

Variants of BspZ00258 (SEQ ID NO: 22) subtilisin containing one, two,three or four amino acid substitutions at positions of interest toincrease enzyme stability, were evaluated for detergent stability andcleaning performance using methods described in Example 2. The BspZ00258subtilisin was previously described as SEQ ID NO:9 in WO 2016069552patent application, and is a member of the BspM04284-clade ofsubtilisins. Table 38 shows the results for BspZ00258 variants.

TABLE 38 BspZ00258 subtilisin variants with improved stability in liquiddetergent at 62° C. (reported as percent residual activity, % RA)compared to BspZ00258 parent Cleaning performance, PI BspZ00258 VariantSubstitutions in Substitutions in BMI stain in PAS-38 stain in Sample IDBspZ00258 numbering BPN′ numbering % RA PNB detergent GSM-B detergentBspZ00258 — — 57 1.0 1.0 BspZ00258-00124 E003V E003V 84 0.6 1.1BspZ00258-00027 G166Q G166Q 78 0.5 1.1 BspZ00258-00045 D259P D259P 660.9 1.6 BspZ00258-00098 A068S-N185Q A069S-N185Q 67 0.8 1.3BspZ00258-00429 A068S-N218S A069S-N218S 61 1.0 1.6 BspZ00258-00244A128P-D259P A129P-D259P 76 0.9 1.4 BspZ00258-00338 G166Q-N185QG166Q-N185Q 78 0.7 1.1 BspZ00258-00106 G166Q-D259P G166Q-D259P 72 0.81.3 BspZ00258-00476 E003V-A068S-G127S E003V-A069S-G128S 90 0.9 1.6BspZ00258-00565 E003V-G127S-D259P E003V-G128S-D259P 88 2.3 3.4BspZ00258-00337 E003V-A128P-N185Q E003V-A129P-N185Q 88 0.7 1.4BspZ00258-00538 A068S-A128P-G166Q A069S-A129P-G166Q 79 0.8 1.2BspZ00258-00095 E003V-A068S- E003V-A069S- 90 1.2 2.6 G127S-N185QG128S-N185Q BspZ00258-00020 E003V-A068S- E003V-A069S- 88 0.8 2.0A128P-N185Q A129P-N185Q BspZ00258-00145 E003V-G127S- E003V-G128S- 93 1.52.7 N185Q-D259P N185Q-D259P BspZ00258-00096 E003V-A128P- E003V-A129P- 860.7 1.6 N185Q-N218S N185Q-N218S

Example 21 BspZ00056 Subtilisin Variants with Improved Stability inDetergent

Variants of BspZ00056 (SEQ ID NO:17) subtilisin containing three or fouramino acid substitutions at positions of interest to increase enzymestability, were generated using methods similar to the ones described inExample 1. These variant samples were evaluated for detergent stabilityand cleaning performance using methods described in Example 2. Table 39Aand 39B show the results for BspZ00056 variants.

TABLE 39A BspZ00056 subtilisin variants with improved stability inliquid detergent at 64° C. (reported as percent residual activity, % RA)compared to BspZ00056 parent Cleaning performance, PI BspZ00056 VariantSubstitutions in Substitutions in BMI stain in PAS-38 stain in Sample IDBspZ00056 numbering BPN′ numbering % RA PNB detergent GSM-B detergentBspZ00056 — — 23 1.0 1.0 BspZ00056-00318 T003V-S133P-G171QT003V-S129P-G166Q 84 1.0 0.6 BspZ00056-00428 T003V-S133P-N190QT003V-S129P-N185Q 61 1.2 0.7 BspZ00056-00131 T003V-S133P-G264PT003V-S129P-G259P 80 1.3 0.8 BspZ00056-00223 T003V-N190Q-N223ST003V-N185Q-N218S 46 1.3 0.2 BspZ00056-00474 A073S-G132S-N190QA069S-G128S-N185Q 74 1.1 0.2 BspZ00056-00104 A073S-S133P-G264PA069S-S129P-G259P 86 1.3 0.4 BspZ00056-00110 A073S-G171Q-N190QA069S-G166Q-N185Q 80 1.3 0.7 BspZ00056-00500 A073S-G171Q-N223SA069S-G166Q-N218S 82 1.5 0.7 BspZ00056-00113 M128I-S133P-N190QM124I-S129P-N185Q 67 1.3 0.3 BspZ00056-00198 M128I-S133P-G264PM124I-S129P-G259P 88 1.3 0.2 BspZ00056-00303 M128I-N190Q-G264PM124I-N185Q-G259P 85 1.2 0.2 BspZ00056-00264 M128I-N223S-G264PM124I-N218S-G259P 89 1.3 0.1 BspZ00056-00302 G132S-G171Q-G264PG128S-G166Q-G259P 85 1.2 0.6 BspZ00056-00483 G132S-N190Q-G264PG128S-N185Q-G259P 100 1.4 0.6 BspZ00056-00238 G171Q-N223S-G264PG166Q-N218S-G259P 87 1.1 0.7 BspZ00056-00334 T003V-A073S- T003V-A069S-75 1.6 0.2 G132S-N190Q G128S-N185Q BspZ00056-00482 T003V-A073S-T003V-A069S- 81 1.8 0.6 N190Q-G264P N185Q-G259P BspZ00056-00498T003V-A073S- T003V-A069S- 75 1.5 0.3 N223S-G264P N218S-G259PBspZ00056-00021 T003V-M128I- T003V-M124I- 89 1.3 0.3 G171Q-G264PG166Q-G259P BspZ00056-00041 T003V-N190Q- T003V-N185Q- 78 1.5 0.3N223S-G264P N218S-G259P BspZ00056-00376 A073S-S133P- A069S-S129P- 85 1.00.5 G171Q-G264P G166Q-G259P BspZ00056-00308 M128I-S133P- M124I-S129P- 911.0 0.2 G171Q-G264P G166Q-G259P BspZ00056-00158 M128I-G171Q-M124I-G166Q- 90 1.1 0.3 N223S-G264P N218S-G259P BspZ00056-00409M128I-N190Q- M124I-N185Q- 95 1.0 0.2 N223S-G264P N218S-G259PBspZ00056-00155 G132S-S133P- G128S-S129P- 90 1.2 0.5 G171Q-G264PG166Q-G259P BspZ00056-00012 S133P-G171Q- S129P-G166Q- 84 1.5 0.8N190Q-G264P N185Q-G259P

TABLE 39B BspZ00056 subtilisin variants with improved stability inliquid detergent at 64° C. (reported as percent residual activity, % RA)compared to BspZ00056 parent BspZ00056 Variant Substitutions inSubstitutions in Sample ID Backbone Numbering BPN′ Numbering % RABspZ00056 — — 30 BspZ00056-00909 T003V-P009E-G171Q T003V-P009E-G166Q 74BspZ00056-00859 T003V-A073S-G171Q T003V-A069S-G166Q 72 BspZ00056-00848T003V-A073S-G264P T003V-A069S-G259P 92 BspZ00056-00808 T003V-G171Q-N190QT003V-G166Q-N185Q 68 BspZ00056-00785 T003V-G171Q-N223S T003V-G166Q-N218S78 BspZ00056-00786 T003V-G171Q-G264P T003V-G166Q-G259P 93BspZ00056-00891 T003V-N190Q-G264P T003V-N185Q-G259P 75 BspZ00056-00787T003V-N223S-G264P T003V-N218S-G259P 79 BspZ00056-00810 P009E-A073S-G171QP009E-A069S-G166Q 67 BspZ00056-01468 P009E-A073S-G264P P009E-A069S-G259P87 BspZ00056-00783 P009E-G171Q-N190Q P009E-G166Q-N185Q 73BspZ00056-00913 P009E-G171Q-N223S P009E-G166Q-N218S 75 BspZ00056-01238P009E-G171Q-G264P P009E-G166Q-G259P 91 BspZ00056-00884 P009E-N223S-G264PP009E-N218S-G259P 82 BspZ00056-00704 A073S-G171Q-G264P A069S-G166Q-G259P87 BspZ00056-00693 A073S-N190Q-G264P A069S-N185Q-G259P 78BspZ00056-00705 A073S-N223S-G264P A069S-N218S-G259P 90 BspZ00056-00710G171Q-N190Q-G264P G166Q-N185Q-G259P 69 BspZ00056-01490 N190Q-N223S-G264PN185Q-N218S-G259P 98 BspZ00056-01432 T003V-P009E-A073S-G171QT003V-P009E-A069S-G166Q 86 BspZ00056-01158 T003V-P009E-G171Q-G264PT003V-P009E-G166Q-G259P 100 BspZ00056-01153 T003V-A073S-G171Q-N190QT003V-A069S-G166Q-N185Q 90 BspZ00056-01078 T003V-G171Q-N223S-G264PT003V-G166Q-N218S-G259P 97 BspZ00056-01084 P009E-A073S-G171Q-N223SP009E-A069S-G166Q-N218S 79 BspZ00056-01115 P009E-G171Q-N190Q-N223SP009E-G166Q-N185Q-N218S 82 BspZ00056-01032 P009E-G171Q-N190Q-G264PP009E-G166Q-N185Q-G259P 100 BspZ00056-01179 P009E-G171Q-N223S-G264PP009E-G166Q-N218S-G259P 87 BspZ00056-01233 P009E-N190Q-N223S-G264PP009E-N185Q-N218S-G259P 79 BspZ00056-01152 A073S-G171Q-N190Q-N223SA069S-G166Q-N185Q-N218S 82 BspZ00056-01379 A073S-G171Q-N190Q-G264PA069S-G166Q-N185Q-G259P 83 BspZ00056-01194 A073S-G171Q-N223S-G264PA069S-G166Q-N218S-G259P 92 BspZ00056-01234 G171Q-N190Q-N223S-G264PG166Q-N185Q-N218S-G259P 100

Example 22 Globally Beneficial Stability Mutations in Subtilisins

Analysis of improved detergent stability results across the followingbackbones: AprE (subtilisin E, SEQ ID NO:8); Chemgen_164A (SEQ IDNO:10); Bpan01744 (SEQ ID NO:13); DSM14391 (SEQ ID NO:14); BspAI02518(SEQ ID NO:16); BspZ00056 (SEQ ID NO:17); Bba02069 (SEQ ID NO:19); CP474(SEQ ID NO:11) and ZP-00454 (SEQ ID NO:12) was performed. Variantscomprising 1 or 2 substitutions on the wild-type backbone are shown inTable 40. At least half of all possible double combinations of thefollowing features: X003V, X009E, X040E, X069S, X076D, X078N, X166Q,X185Q, X218S, and X259P introduced into the 9 backbones listed aboveshowed increased stability for singly or doubly substituted variants.Variants comprising 3 substitutions on the wild-type backbone are shownon Table 41. At least half of all possible triple combinations of thefollowing features: X003V, X009E, X040E, X069S, X076D, X078N, X166Q,X185Q, X218S, and X259P introduced into the following 7 backbones AprE(subtilisin E, SEQ ID NO:8); Chemgen_164A (SEQ ID NO:10); Bpan01744 (SEQID NO:13); DSM14391 (SEQ ID NO:14); BspAI02518 (SEQ ID NO:16); BspZ00056(SEQ ID NO:17); Bba02069 (SEQ ID NO:19) showed increased stability fortriply substituted variants.

In Tables 40 and 41, the term “shared feature” corresponds to amino acidposition of interest where a substitution was introduced, or in somecases the amino acid of interest is naturally occurring. Sample IDs onTable 40 are as follows: variants of AprE have an AprE suffix, variantsof Chemgen_164A have a Chemgen suffix, variants of DSM14391 have aDSM14391 suffix, variants of BspZ00056 have a BspZ00056 suffix, variantsof Bba02069 have a Bba02069 suffix, variants of BspAI02518 have aBspAI02518 suffix, variants of Bpan01744 have a Bpan01744 suffix,variants of CP474 have a CP474 suffix, and variants of ZP-00454 have aZP-00454 suffix. All substitutions are listed based on correspondingpositions in BPN′ numbering (SEQ ID NO: 1) according to multiple proteinsequence alignment shown in Table 28.

TABLE 40 Variants of AprE, Chemgen, DSM14391, BspZ00056, Bba02069,BspAI02518, Bpan01744, CP474, and ZP-00454 subtilisins with sharedfeatures Shared feature in BPN′ numbering Variants with shared featureX003V-X009E AprE-01089, Chemgen-00795, Bpan01744-00830, DSM14391-00986,BspAI02518-01175, Bba02069-00854 X003V-X040E AprE-00380, Chemgen-00794,CP474-00592, ZP-00454-00011, Bpan01744-00498, DSM14391-00987,BspAI02518-00709, Bba02069- 00855, BspZ00056-00876 X003V-X069SAprE-01078, Chemgen-00481, CP474-00602, ZP-00454-00021, Bpan01744-00167,DSM14391-00025, BspAI02518-00599, Bba02069- 00030, BspZ00056-00094X003V-X076D AprE-00729, Chemgen-00076, CP474-00571, ZP-00454-00031,Bpan01744-00166, DSM14391-00340, BspAI02518-00897, Bba02069- 00564,BspZ00056-00876 X003V-X078N AprE-00515, Chemgen-00443, CP474-00612,ZP-00454-00041, Bpan01744-00304, DSM14391-00373, BspAI02518-01179,Bba02069-00652 X003V-X166Q AprE-00841, Chemgen-00378, CP474-00563,Bpan01744-01145, DSM14391-00028, BspAI02518-00959, Bba02069-00347,BspZ00056-00221 X003V-X185Q AprE-00772, Chemgen-00108, CP474-00573,Bpan01744-00152, DSM14391-00016, BspAI02518-00624, Bba2069-00121,BspZ00056-00116 X003V-X218S AprE-01842, Chemgen-00634, CP474-00583,Bpan01744-00417, DSM14391-00492, BspAI02518-00564, Bba02069-00856,BspZ00056-00368 X003V-X259P AprE-00370, Chemgen-00650, CP474-00593,Bpan01744-00544, DSM14391-00063, BspAI02518-00506, Bba02069-00477,BspZ00056-00384 X009E-X040E AprE-01082, Bpan01744-02141, DSM14391-00863,BspAI02518-00637, Bba02069-00755, BspZ00056-01485 X009E-X069SAprE-01083, Chemgen-00788, DSM14391-00864, BspAI02518-01198,Bba02069-00756 X009E-X076D AprE-01025, Chemgen-00712, Bpan01744-01257,DSM14391-00839, BspAI02518-01178, Bba02069-00757, BspZ00056-01485X009E-X078N AprE-01850, Chemgen-00714, Bpan01744-02075, DSM14391-00962,BspAI02518-01186, Bba02069-00654 X009E-X166Q AprE-01959, Chemgen-00797,Bpan01744-01122, BspAI02518-01991, Bba02069-00871, BspZ00056-01478X009E-X185Q AprE-01081, Chemgen-00798, Bpan01744-01123, DSM14391-01005,BspAI02518-01187, Bba02069-00866 X009E-X218S AprE-01111,Bpan01744-00795, DSM14391-00971, BspAI02518-01811, Bba02069-00865X009E-X259P AprE-01096, Chemgen-00741, Bpan01744-01124, DSM14391-00867,BspAI02518-02004, Bba02069-00758, BspZ00056-00875 X040E-X069SAprE-01951, CP474-00603, ZP-00454-00052, DSM14391-00968, Bba02069-00863,BspZ00056-00863 X040E-X076D AprE-01108, CP474-00581, ZP-00454-00062,Bpan01744-01310, DSM14391-00969, BspAI02518-00689, Bba02069-00824X040E-X078N AprE-01844, Chemgen-00715, CP474-00613, ZP-00454-00072,Bpan01744-00574, DSM14391-00217, BspAI02518-00585, Bba02069-00653X040E-X166Q AprE-01107, Chemgen-01467, CP474-00564, ZP-00454-00043,BspAI02518-01177, Bba02069-00499, BspZ00056-00864 X040E-X185QAprE-01080, Chemgen-00716, CP474-00574, ZP-00454-00053, Bpan01744-00717,DSM14391-00985, BspAI02518-00764, Bba02069- 00377, BspZ00056-00663X040E-X218S AprE-01054, Chemgen-01219, CP474-00584, ZP-00454-00063,Bpan01744-00892, DSM14391-00977, BspAI02518-00819, Bba02069- 01952,BspZ00056-00248 X040E-X259P AprE-01105, CP474-00594, ZP-00454-00073,Bpan01744-01737, DSM14391-00849, BspAI02518-00838, Bba02069-00845,BspZ00056-00819 X069S-X076D AprE-00498, Chemgen-00527, CP474-00591,ZP-00454-00004, Bpan01744-00088, DSM14391-00494, BspAI02518-00412,Bba02069- 00518, BspZ00056-00863 X069S-X078N AprE-00788, Chemgen-00436,CP474-00604, ZP-00454-00014, Bpan01744-00423, DSM14391-00005,BspAI02518-00590, Bba02069- 00648, BspZ00056-00490 X069S-X166QAprE-00666, Chemgen-00394, CP474-00634, Bpan01744-00153,BspAI02518-01025, Bba02069-00505, BspZ00056-00389 X069S-X185QChemgen-00617, CP474-00565, ZP-00454-00074, Bpan01744-00414,DSM14391-00136, BspAI02518-00646, Bba02069-00844, BspZ00056-00042X069S-X218S AprE-00594, Chemgen-00569, ZP-00454-00005, Bpan01744-00488,DSM14391-00432, BspAI02518-00405, Bba02069-00736, BspZ00056-00873X069S-X259P AprE-00758, Chemgen-00444, DSM14391-00096, BspAI02518-01920,Bba02069-00114, BspZ00056-00151 X076D-X078N AprE-00774, Chemgen-00459,CP474-00601, ZP-00454-00025, Bpan01744-00337, DSM14391-00007,BspAI02518-00814, Bba02069-00644 X076D-X166Q AprE-00920, Chemgen-00132,CP474-00631, ZP-00454-00075, Bpan01744-01035, BspAI02518-01184,Bba02069-00247, BspZ00056-00864 X076D-X185Q AprE-00795, Chemgen-00804,CP474-00562, ZP-00454-00006, Bpan01744-01133, DSM14391-00974,BspAI02518-00802, Bba02069- 00822, BspZ00056-00663 X076D-X218SAprE-00912, Chemgen-00367, ZP-00454-00016, Bpan01744-01135,DSM14391-00168, BspAI02518-00535, Bba02069-00815, BspZ00056-00248X076D-X259P AprE-01836, Chemgen-00546, ZP-00454-00026, Bpan01744-01148,DSM14391-00976, BspAI02518-00695, Bba02069-00423, BspZ00056-00819X078N-X166Q AprE-00974, Chemgen-00560, CP474-00615, ZP-00454-00076,Bpan01744-00158, BspAI02518-01190, Bba02069-00111, BspZ00056-00297X078N-X185Q AprE-00488, Chemgen-00224, CP474-00625, ZP-00454-00007,Bpan01744-01629, DSM14391-00302, BspAI02518-01032 X078N-X218SAprE-00904, Chemgen-00313, CP474-00635, Bpan01744-00991, DSM14391-00252,BspAI02518-00800, Bba02069-00655 X078N-X259P AprE-00891, Chemgen-00350,CP474-00566, ZP-00454-00027, Bpan01744-01151, DSM14391-00113,BspAI02518-00937, Bba02069- 00217, BspZ00056-00088 X166Q-X185QAprE-00944, Chemgen-00122, Bpan01744-00369, DSM14391-00171,BspAI02518-02195, Bba02069-00190, BspZ00056-00257 X166Q-X218SAprE-00698, Chemgen-00335, CP474-00597, Bpan01744-00172, DSM14391-00828,BspAI02518-01002, Bba02069-00817, BspZ00056-00837 X166Q-X259PAprE-00694, Chemgen-00010, Bpan01744-00048, DSM14391-00430,BspAI02518-01006, Bba02069-00043, BspZ00056-00133 X185Q-X218SAprE-00924, Chemgen-00198, CP474-00617, Bpan01744-00094, DSM14391-00161,BspAI02518-01094, Bba02069-00493, BspZ00056-01030 X185Q-X259PAprE-00447, Chemgen-00359, CP474-00579, Bpan01744-00339, DSM14391-00203,BspAI02518-00439, Bba02069-00005, BspZ00056-00377 X218S-X259PAprE-00646, Chemgen-00309, CP474-00627, Bpan01744-00126, DSM14391-00844,BspAI02518-00548, Bba02069-00051, BspZ00056-00491

TABLE 41 Variants of AprE, Chemgen, DSM14391, BspZ00056, Bba02069,BspAI02518, and Bpan01744 subtilisins with shared features Sharedfeature in BPN′ numbering Variants with shared feature X003V-X009E-X040EAprE-01102, Chemgen-00801, Bpan01744-00830, DSM14391- 00824,BspAI02518-01175, Bba02069-00812 X003V-X009E-X069S AprE-01101,Chemgen-01562, Bpan01744-01709, DSM14391- 00996, BspAI02518-01092,Bba02069-00811 X003V-X009E-X076D AprE-01051, Bpan01744-01195,DSM14391-00995, BspAI02518- 01095, Bba02069-00809 X003V-X009E-X078NAprE-01099, Bpan01744-01267, DSM14391-00823, BspAI02518- 01270,Bba02069-00854 X003V-X009E-X166Q AprE-01045, BspAI02518-01096,Bba02069-00744, BspZ00056-00909 X003V-X009E-X185Q AprE-01089,Chemgen-00792, Bpan01744-01140, DSM14391- 00868, BspAI02518-01276,Bba02069-00808 X003V-X009E-X218S AprE-01077, Bpan01744-01141,DSM14391-00822, BspAI02518- 01097, Bba02069-00829 X003V-X009E-X259PAprE-01047, Bpan01744-01315, DSM14391-00817, BspAI02518- 01282,Bba02069-00843 X003V-X040E-X069S AprE-01009, Bpan01744-00167,DSM14391-00836, BspAI02518- 00599, Bba02069-00747, BspZ00056-00094X003V-X040E-X076D AprE-01048, Chemgen-01640, Bpan01744-00166, DSM14391-00819, BspAI02518-00897, Bba02069-00833 X003V-X040E-X078NBpan01744-00304, DSM14391-00837, BspAI02518-01179, Bba02069-00855X003V-X040E-X166Q Chemgen-00793, Bpan01744-01145, BspAI02518-00959,Bba02069-00013, BspZ00056-00221 X003V-X040E-X185Q AprE-00380,Chemgen-01651, Bpan01744-00152, DSM14391- 01004, BspAI02518-00624,Bba02069-00664, BspZ00056-00116 X003V-X040E-X218S AprE-01915,Bpan01744-00417, DSM14391-00421, BspAI02518- 00564, Bba02069-00781,BspZ00056-00368 X003V-X040E-X259P AprE-01039, Chemgen-00724,Bpan01744-00544, DSM14391- 00829, BspAI02518-00506, Bba02069-00834,BspZ00056-00384 X003V-X069S-X076D AprE-01864, Chemgen-00816,Bpan01744-00169, DSM14391- 00831, BspAI02518-01085, Bba02069-00779,BspZ00056-00094 X003V-X069S-X078N AprE-01056, Chemgen-00808,Bpan01744-01142, BspAI02518- 01086, Bba02069-00030 X003V-X069S-X166QAprE-00991, Chemgen-00807, Bba02069-00778, BspZ00056-00859X003V-X069S-X185Q AprE-01078, Chemgen-01642, Bpan01744-00150, DSM14391-00858, BspAI02518-00534 X003V-X069S-X218S AprE-01060, Chemgen-00727,Bpan01744-00677, DSM14391- 00992, BspAI02518-01087, Bba02069-00679X003V-X069S-X259P AprE-01064, Chemgen-01658, Bba02069-00776,BspZ00056-00848 X003V-X076D-X078N AprE-00685, Chemgen-00729,Bpan01744-01265, DSM14391- 00833, BspAI02518-01088, Bba02069-00564X003V-X076D-X166Q AprE-01340, Chemgen-00694, Bpan01744-01585,BspAI02518- 01250, Bba02069-00836, BspZ00056-00221 X003V-X076D-X185QAprE-00729, Chemgen-00776, Bpan01744-00170, DSM14391- 01080,BspAI02518-01084, Bba02069-00827, BspZ00056-00116 X003V-X076D-X218SAprE-01867, Chemgen-00775, Bpan01744-01252, DSM14391- 01084,BspAI02518-01220, Bba02069-00825, BspZ00056-00368 X003V-X076D-X259PAprE-01062, Chemgen-00832, DSM14391-01058, BspAI02518- 01230,Bba02069-00842, BspZ00056-00384 X003V-X078N-X166Q Chemgen-00774,Bpan01744-00059, BspAI02518-01222, Bba02069-00347 X003V-X078N-X185QAprE-00515, Chemgen-00696, Bpan01744-01253, DSM14391- 00922,BspAI02518-01895, Bba02069-00121 X003V-X078N-X218S AprE-00353,Bpan01744-01254, DSM14391-01083, BspAI02518- 01231, Bba02069-00856X003V-X078N-X259P AprE-01068, Chemgen-00834, Bpan01744-01260, DSM14391-01054, BspAI02518-01992, Bba02069-00477 X003V-X166Q-X185Q AprE-00841,Chemgen-00738, BspAI02518-01110, Bba02069- 00760, BspZ00056-00808X003V-X166Q-X218S AprE-00773, Bpan01744-00547, DSM14391-00214, Bba02069-00840, BspZ00056-00785 X003V-X166Q-X259P AprE-01855, Chemgen-00739,DSM14391-00359, BspAI02518- 02118, Bba02069-00471, BspZ00056-00786X003V-X185Q-X218S AprE-01842, Chemgen-00785, Bpan01744-01274, DSM14391-00929, BspAI02518-01099, BspZ00056-00223 X003V-X185Q-X259P AprE-00370,Chemgen-00698, Bpan01744-00685, DSM14391- 01078, BspAI02518-00539,Bba02069-00838, BspZ00056-00891 X003V-X218S-X259P AprE-00753,Chemgen-00780, Bpan01744-01275, DSM14391- 00919, BspAI02518-01960,Bba02069-00764, BspZ00056-00787 X009E-X040E-X069S AprE-01674,Chemgen-01553, BspAI02518-01198, Bba02069-00846 X009E-X040E-X076DAprE-01069, Chemgen-00703, Bpan01744-01257, DSM14391- 00931,BspAI02518-01178, Bba02069-00886 X009E-X040E-X078N AprE-01997,Chemgen-00683, Bpan01744-02075, DSM14391- 00928, BspAI02518-01186,Bba02069-00755 X009E-X040E-X166Q AprE-01984, Chemgen-00702,Bpan01744-01122, BspAI02518- 01991, Bba02069-00847, BspZ00056-01478X009E-X040E-X185Q AprE-01082, Bpan01744-01123, DSM14391-01025,BspAI02518- 01187, Bba02069-01933 X009E-X040E-X218S AprE-01529,Chemgen-00822, Bpan01744-00795, DSM14391- 01034, BspAI02518-01811,Bba02069-01674 X009E-X040E-X259P AprE-01125, Chemgen-01604,Bpan01744-01124, DSM14391- 00899, BspAI02518-02004, Bba02069-00763,BspZ00056-00875 X009E-X069S-X076D AprE-01071, Chemgen-00684,Bpan01744-00693, BspAI02518- 01238, Bba02069-00848 X009E-X069S-X078NAprE-01091, Chemgen-00700, Bpan01744-00777, DSM14391- 01035,Bba02069-00756 X009E-X069S-X166Q AprE-01871, Chemgen-00823,Bpan01744-00898, Bba02069-00849, BspZ00056-00810 X009E-X069S-X185QAprE-01083, BspAI02518-01102, Bba02069-00791 X009E-X069S-X218SAprE-01087, Chemgen-00681, DSM14391-01030, BspAI02518- 01165,Bba02069-00722 X009E-X069S-X259P AprE-01857, Chemgen-00829,Bpan01744-01231, DSM14391- 01042, Bba02069-00795, BspZ00056-01468X009E-X076D-X078N AprE-01892, Chemgen-00825, Bpan01744-01236, DSM14391-01040, BspAI02518-01105, Bba02069-00757 X009E-X076D-X166Q AprE-01093,Chemgen-01315, Bpan01744-01237, BspAI02518- 01235, Bba02069-00796,BspZ00056-01478 X009E-X076D-X185Q AprE-01025, Chemgen-00737,Bpan01744-01238, DSM14391- 00908, BspAI02518-01153, Bba02069-00725X009E-X076D-X218S AprE-01052, Chemgen-00690, Bpan01744-01196, DSM14391-01038, BspAI02518-02121, Bba02069-01905 X009E-X076D-X259P AprE-01860,Chemgen-01420, Bpan01744-01307, DSM14391- 01049, BspAI02518-01107,Bba02069-00793, BspZ00056-00875 X009E-X078N-X166Q AprE-01095,Chemgen-00826, BspAI02518-02083, Bba02069-00871 X009E-X078N-X185QAprE-01850, Chemgen-01162, Bpan01744-01248, DSM14391- 00915,BspAI02518-01268, Bba02069-00866 X009E-X078N-X218S AprE-01019,Chemgen-00688, Bpan01744-01241, DSM14391- 01047, BspAI02518-01140,Bba02069-00865 X009E-X078N-X259P AprE-01014, Chemgen-00818,Bpan01744-01242, DSM14391- 01053, BspAI02518-01142, Bba02069-00758X009E-X166Q-X185Q AprE-01959, Bpan01744-01165, BspAI02518-01167,Bba02069- 00794, BspZ00056-00783 X009E-X166Q-X218S AprE-01029,Chemgen-00687, Bpan01744-01244, DSM14391- 01043, BspAI02518-01138,Bba02069-00797, BspZ00056-00913 X009E-X166Q-X259P AprE-01028,Chemgen-00686, BspAI02518-01226, Bba02069- 00715, BspZ00056-01238X009E-X185Q-X218S AprE-01111, Chemgen-00705, Bpan01744-00976, DSM14391-00911, BspAI02518-01227, Bba02069-00799 X009E-X185Q-X259P AprE-01096,Chemgen-00685, Bpan01744-01351, DSM14391- 00912, BspAI02518-01148,Bba02069-00718 X009E-X218S-X259P AprE-01026, Bpan01744-01157,DSM14391-01045, BspAI02518- 01251, Bba02069-00801, BspZ00056-00884X040E-X069S-X076D Chemgen-00878, Bpan01744-00088, DSM14391-01074,BspAI02518-00412, Bba02069-00720 X040E-X069S-X078N AprE-01024,Chemgen-00876, Bpan01744-00423, BspAI02518- 00590, Bba02069-00863,BspZ00056-00490 X040E-X069S-X166Q AprE-01865, Chemgen-00868,Bpan01744-00153, BspAI02518- 01025, Bba02069-00802, BspZ00056-00389X040E-X069S-X185Q AprE-01951, Bpan01744-00414, DSM14391-00689,BspAI02518- 00646, Bba02069-01826, BspZ00056-00042 X040E-X069S-X218SAprE-01823, Bpan01744-00488, DSM14391-01032, BspAI02518- 00405,Bba02069-00882, BspZ00056-00873 X040E-X069S-X259P AprE-01036,Chemgen-01310, DSM14391-01033, BspAI02518- 01920, Bba02069-00730,BspZ00056-00151 X040E-X076D-X078N AprE-00540, Chemgen-00761,Bpan01744-00337, DSM14391- 01352, BspAI02518-00814, Bba02069-00824X040E-X076D-X166Q AprE-01032, Chemgen-00642, Bpan01744-01035, DSM14391-00272, BspAI02518-01184, Bba02069-00693 X040E-X076D-X185Q AprE-01108,Chemgen-00660, Bpan01744-01133, DSM14391- 00469, BspAI02518-00802,Bba02069-00729 X040E-X076D-X218S AprE-01824, Chemgen-00641,Bpan01744-01135, DSM14391- 00953, BspAI02518-00535, Bba02069-00695X040E-X076D-X259P AprE-01031, Bpan01744-01148, DSM14391-00686,BspAI02518- 00695, Bba02069-00696 X040E-X078N-X166Q AprE-01825,Bpan01744-00158, BspAI02518-01190, Bba02069- 00499, BspZ00056-00297X040E-X078N-X185Q AprE-01844, Chemgen-01465, Bpan01744-01629, DSM14391-01066, BspAI02518-01032, Bba02069-00377 X040E-X078N-X218S AprE-01030,Bpan01744-00991, DSM14391-01065, BspAI02518- 00800, Bba02069-01952X040E-X078N-X259P AprE-01035, Chemgen-00758, Bpan01744-01151, DSM14391-00659, BspAI02518-00937, Bba02069-00845, BspZ00056-00088X040E-X166Q-X185Q AprE-01107, Chemgen-00872, Bpan01744-00369,BspAI02518- 02195, Bba02069-00692, BspZ00056-00257 X040E-X166Q-X218SAprE-01820, Chemgen-00873, Bpan01744-00172, DSM14391- 00947,BspAI02518-01002, Bba02069-00691, BspZ00056-00837 X040E-X166Q-X259PAprE-01831, Chemgen-00752, Bpan01744-00048, BspAI02518- 01006,Bba02069-00705, BspZ00056-00133 X040E-X185Q-X218S AprE-01054,Chemgen-00750, Bpan01744-00094, DSM14391- 00281, BspAI02518-01094,Bba02069-00706, BspZ00056-01030 X040E-X185Q-X259P AprE-01105,Chemgen-00851, Bpan01744-00339, DSM14391- 00293, BspAI02518-00439,Bba02069-00686, BspZ00056-00377 X040E-X218S-X259P AprE-01826,Chemgen-00845, Bpan01744-00126, DSM14391- 00960, BspAI02518-00548,Bba02069-00685, BspZ00056-00491 X069S-X076D-X078N AprE-01810,Chemgen-00844, Bpan01744-00810, DSM14391- 00945, BspAI02518-01243,Bba02069-00518, BspZ00056-00490 X069S-X076D-X166Q AprE-01812,Chemgen-00746, Bpan01744-01159, BspAI02518- 01245, Bba02069-00708,BspZ00056-00389 X069S-X076D-X185Q AprE-00498, Chemgen-00748,Bpan01744-00291, DSM14391- 01016, BspAI02518-01139, Bba02069-00883,BspZ00056-00042 X069S-X076D-X218S AprE-01403, Chemgen-01054,Bpan01744-00736, DSM14391- 01013, BspAI02518-00870, Bba02069-00684,BspZ00056-00873 X069S-X076D-X259P AprE-01829, Chemgen-00744,Bpan01744-00888, DSM14391- 01012, BspAI02518-01219, Bba02069-00683,BspZ00056-00151 X069S-X078N-X166Q AprE-01830, Chemgen-00861,BspAI02518-01205, Bba02069-00505 X069S-X078N-X185Q AprE-00788,Chemgen-00860, Bpan01744-01154, DSM14391- 00883, Bba02069-00844X069S-X078N-X218S AprE-01693, Chemgen-00859, Bpan01744-01162, DSM14391-01014, BspAI02518-01207, Bba02069-00736 X069S-X078N-X259P AprE-01873,Chemgen-00756, Bpan01744-01779, DSM14391- 00474, Bba02069-00114X069S-X166Q-X185Q AprE-00666, Bpan01744-00174, BspAI02518-01166,Bba02069- 00703, BspZ00056-00110 X069S-X166Q-X218S AprE-00996,Chemgen-00862, Bpan01744-01885, DSM14391- 01007, BspAI02518-01201,Bba02069-01832, BspZ00056-00500 X069S-X166Q-X259P AprE-01117,Chemgen-00753, BspAI02518-01151, Bba02069- 00704, BspZ00056-00704X069S-X185Q-X218S AprE-00594, Chemgen-00659, Bpan01744-00963, DSM14391-01105, BspAI02518-01215, Bba02069-01679 X069S-X185Q-X259P AprE-00758,Chemgen-00863, DSM14391-00882, Bba02069-00930, BspZ00056-00693X069S-X218S-X259P AprE-01807, Chemgen-00864, Bpan01744-01174, DSM14391-00264, BspAI02518-01202, Bba02069-00700, BspZ00056-00705X076D-X078N-X166Q AprE-01805, Chemgen-00645, Bpan01744-00228,BspAI02518- 01199, Bba02069-00247, BspZ00056-00297 X076D-X078N-X185QAprE-00774, Bpan01744-01182, DSM14391-01018, BspAI02518- 00999,Bba02069-00822 X076D-X078N-X218S AprE-01407, Chemgen-00865,Bpan01744-01173, DSM14391- 01021, BspAI02518-00507, Bba02069-00815X076D-X078N-X259P AprE-01118, Chemgen-00866, Bpan01744-01957, DSM14391-01019, BspAI02518-01218, Bba02069-00423, BspZ00056-00088X076D-X166Q-X185Q AprE-00920, BspAI02518-01210, Bba02069-00699,BspZ00056-00257 X076D-X166Q-X218S AprE-01802, Chemgen-00770,Bpan01744-01170, DSM14391- 01100, BspAI02518-01211, Bba02069-00698,BspZ00056-00837 X076D-X166Q-X259P AprE-01819, Chemgen-01542,BspAI02518-01212, Bba02069- 01319, BspZ00056-00133 X076D-X185Q-X218SAprE-00912, Chemgen-00771, Bpan01744-01292, DSM14391- 00473,BspAI02518-01124, Bba02069-01333, BspZ00056-01030 X076D-X185Q-X259PAprE-01836, Bpan01744-01289, BspAI02518-01132, Bba02069- 01321,BspZ00056-00377 X076D-X218S-X259P AprE-01817, Chemgen-00846,DSM14391-00162, BspAI02518- 01122, Bba02069-01323, BspZ00056-00491X078N-X166Q-X185Q AprE-00974, Chemgen-00847, BspAI02518-02142,Bba02069-00190 X078N-X166Q-X218S AprE-01722, Chemgen-00763,Bpan01744-01294, DSM14391- 01090, BspAI02518-01128, Bba02069-00817X078N-X166Q-X259P AprE-01816, BspAI02518-01119, Bba02069-00043X078N-X185Q-X218S AprE-00904, Bpan01744-01717, DSM14391-00170,BspAI02518- 01114, Bba02069-00493 X078N-X185Q-X259P AprE-00891,Chemgen-00849, Bpan01744-00034, DSM14391- 01086, BspAI02518-01263,Bba02069-00005 X078N-X218S-X259P AprE-01112, Chemgen-00768,Bpan01744-01952, DSM14391- 00263, BspAI02518-01115, Bba02069-00051X166Q-X185Q-X218S AprE-00698, Chemgen-00765, Bpan01744-00899, DSM14391-00893, BspAI02518-01265, Bba02069-01324 X166Q-X185Q-X259P AprE-00694,Chemgen-00870, BspAI02518-01117, Bba02069- 01335, BspZ00056-00710X166Q-X218S-X259P AprE-01815, Chemgen-00880, DSM14391-01445, BspAI02518-01116, Bba02069-01328, BspZ00056-00238 X185Q-X218S-X259P AprE-00646,Chemgen-00767, Bpan01744-01867, DSM14391- 00872, Bba02069-01329,BspZ00056-01490

Although the disclosure has been described in conjunction with specificembodiments thereof, it is evident that many alternatives, modificationsand variations will be apparent to those skilled in the art.Accordingly, it is intended to embrace all such alternatives,modifications and variations that fall within the spirit and broad scopeof the appended claims.

All publications, patents and patent applications mentioned in thisspecification are herein incorporated in their entirety by referenceinto the specification, to the same extent as if each individualpublication, patent or patent application was specifically andindividually indicated to be incorporated herein by reference. Inaddition, citation or identification of any reference in thisapplication shall not be construed as an admission that such referenceis available as prior art to the present disclosure. To the extent thatsection headings are used, they should not be construed as necessarilylimiting.

We claim:
 1. A subtilisin variant having at least 70% amino acidsequence identity to SEQ ID NO: 8, 9, 10, 11, 12, 13, 14, 15, 16, 17,18, 19, or 22, wherein the variant has at least one, two, three, four,or more features selected from the group consisting of: X003T, X003V,X009E, X024Q, X040E, X069S, X076D, X078N, X079I, X087D, X118R, X124I,X128R, X128S, X129P, X130S, X145R, X166Q, X182E, X185Q, X210I, X211P,X217L, X218S, X248D, and X259P, wherein the positions are numbered bycorrespondence with the amino acid sequence of SEQ ID NO:1 (BPN′),wherein the variant does not have 100% sequence identity to anaturally-occurring amino acid sequence.
 2. The subtilisin variant ofclaim 1, wherein the variant has at least one, two or more featuresselected from the group consisting of X003V, X009E, X024Q, X040E, X069S,X076D, X078N, X079I, X087D, X118R, X124I, X128S, X129P, X130S, X145R,X166Q, X182E, X185Q, X210I, X217L, X218S, X248D, and X259P, wherein thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′), wherein the variant does not have 100% sequenceidentity to a naturally-occurring amino acid sequence.
 3. The subtilisinvariant of claim 1, wherein the variant has at least one, two or morefeatures selected from the group consisting of X003V, X009E, X040E,X069S, X076D, X078N, X166Q, X185Q, X218S, and X259P, wherein thepositions are numbered by correspondence with the amino acid sequence ofSEQ ID NO:1 (BPN′), wherein the variant does not have 100% sequenceidentity to a naturally-occurring amino acid sequence.
 4. The subtilisinvariant of claim 1, wherein the variant has at least one featureselected from the group consisting of, X003V-X009E, X003V-X024Q,X003V-X040E, X003V-X069S, X003V-X076D, X003V-X078N, X003V-X079I,X003V-X087D, X003V-X118R, X003V-X124I, X003V-X128S, X003V-X129P,X003V-X130S, X003V-X145R, X003V-X166Q, X003V-X185Q, X003V-X210I,X003V-X217L, X003V-X218S, X003V-X248D, X003V-X259P, X009E-X024Q,X009E-X040E, X009E-X069S, X009E-X076D, X009E-X078N, X009E-X079I,X009E-X087D, X009E-X118R, X009E-X124I, X009E-X128S, X009E-X129P,X009E-X130S, X009E-X145R, X009E-X166Q, X009E-X185Q, X009E-X210I,X009E-X217L, X009E-X218S, X009E-X248D, X009E-X259P, X024Q-X040E,X024Q-X069S, X024Q-X076D, X024Q-X078N, X024Q-X079I, X024Q-X087D,X024Q-X118R, X024Q-X124I, X024Q-X128S, X024Q-X129P, X024Q-X130S,X024Q-X145R, X024Q-X166Q, X024Q-X185Q, X024Q-X210I, X024Q-X217L,X024Q-X218S, X024Q-X248D, X024Q-X259P, X040E-X069S, X040E-X076D,X040E-X078N, X040E-X079I, X040E-X087D, X040E-X118R, X040E-X124I,X040E-X128S, X040E-X129P, X040E-X130S, X040E-X145R, X040E-X166Q,X040E-X185Q, X040E-X210I, X040E-X217L, X040E-X218S, X040E-X248D,X040E-X259P, X069S-X076D, X069S-X078N, X069S-X079I, X069S-X087D,X069S-X118R, X069S-X124I, X069S-X128S, X069S-X129P, X069S-X130S,X069S-X145R, X069S-X166Q, X069S-X185Q, X069S-X210I, X069S-X217L,X069S-X218S, X069S-X248D, X069S-X259P, X076D-X078N, X076D-X079I,X076D-X087D, X076D-X118R, X076D-X124I, X076D-X128S, X076D-X129P,X076D-X130S, X076D-X145R, X076D-X166Q, X076D-X185Q, X076D-X210I,X076D-X217L, X076D-X218S, X076D-X248D, X076D-X259P, X078N-X079I,X078N-X087D, X078N-X118R, X078N-X124I, X078N-X128S, X078N-X129P,X078N-X130S, X078N-X145R, X078N-X166Q, X078N-X185Q, X078N-X210I,X078N-X217L, X078N-X218S, X078N-X248D, X078N-X259P, X079I-X087D,X079I-X118R, X079I-X124I, X079I-X128S, X079I-X129P, X079I-X130S,X079I-X145R, X079I-X166Q, X079I-X185Q, X079I-X210I, X079I-X217L,X079I-X218S, X079I-X248D, X079I-X259P, X087D-X118R, X087D-X124I,X087D-X128S, X087D-X129P, X087D-X130S, X087D-X145R, X087D-X166Q,X087D-X185Q, X087D-X210I, X087D-X217L, X087D-X218S, X087D-X248D,X087D-X259P, X118R-X124I, X118R-X128S, X118R-X129P, X118R-X130S,X118R-X145R, X118R-X166Q, X118R-X185Q, X118R-X210I, X118R-X217L,X118R-X218S, X118R-X248D, X118R-X259P, X124I-X128S, X124I-X129P,X124I-X130S, X124I-X145R, X124I-X166Q, X124I-X185Q, X124I-X210I,X124I-X217L, X124I-X218S, X124I-X248D, X124I-X259P, X128S-X129P,X128S-X130S, X128S-X145R, X128S-X166Q, X128S-X185Q, X128S-X210I,X128S-X217L, X128S-X218S, X128S-X248D, X128S-X259P, X129P-X130S,X129P-X145R, X129P-X166Q, X129P-X185Q, X129P-X210I, X129P-X217L,X129P-X218S, X129P-X248D, X129P-X259P, X130S-X145R, X130S-X166Q,X130S-X185Q, X130S-X210I, X130S-X217L, X130S-X218S, X130S-X248D,X130S-X259P, X145R-X166Q, X145R-X185Q, X145R-X210I, X145R-X217L,X145R-X218S, X145R-X248D, X145R-X259P, X166Q-X185Q, X166Q-X210I,X166Q-X217L, X166Q-X218S, X166Q-X248D, X166Q-X259P, X185Q-X210I,X185Q-X217L, X185Q-X218S, X185Q-X248D, X185Q-X259P, X210I-X217L,X210I-X218S, X210I-X248D, X210I-X259P, X217L-X218S, X217L-X248D,X217L-X259P, X218S-X248D, X218S-X259P, X248D-X259P wherein the positionsare numbered by correspondence with the amino acid sequence of SEQ IDNO:1 (BPN′), wherein the variant does not have 100% sequence identity toa naturally-occurring amino acid sequence.
 5. The subtilisin variant ofany of the preceding claims, wherein said variant is derived from aparent or reference polypeptide having has 70%, 75%, 80%, 85%, 86%, 87%,88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%amino acid sequence identity to the amino acid sequence of SEQ ID NO: 8,9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or
 22. 6. The subtilisinvariant of any of the preceding claims, wherein said variant comprisesan amino acid sequence having 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%,91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% amino acid sequenceidentity to the amino acid sequence of SEQ ID NO: 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, or
 22. 7. The subtilisin variant of anypreceding claim, wherein said variant has improved stability whencompared to a reference subtilisin lacking the one, two, three, four ormore features.
 8. The subtilisin variant of claim 7, wherein theimproved stability is measured as (i) a performance index (PI) of 1.1 orgreater after 20 minutes at 30-70 degrees Celsius in a 10% detergentsolution in comparison to the respective parent or (ii) an improvedresidual activity of at least 10% greater in comparison to therespective parent under the same assay conditions.
 9. The subtilisinvariant of claim 8, wherein the improved stability is measured as (i) aPI of 1.1 or greater after 20 minutes at 30-70 degrees Celsius in 10%detergent solution without protease-stabilizers in comparison to therespective parent or (ii) an improved residual activity of at least 10%greater in comparison to the respective parent under the same assayconditions in a 10% detergent solution without protease-stabilizers. 10.The subtilisin variant of any preceding claim, wherein the subtilisinvariant has protease activity.
 11. The subtilisin variant of claim 10,wherein the subtilisin variant has a cleaning performance index (PI)value of 1.0 or greater in comparison to a reference subtilisin.
 12. Apolynucleotide comprising a nucleotide sequence that encodes thesubtilisin variant of any one of claims 1-11, wherein saidpolynucleotide is optionally isolated.
 13. An expression vector orcassette comprising the polynucleotide of claim
 12. 14. The expressionvector or cassette of claim 13, wherein the polynucleotide is operablylinked to a promoter.
 15. A recombinant host cell comprising the vectoror cassette of claim 13 or
 14. 16. A composition comprising one or moresubtilisin variant according to any preceding claim.
 17. The compositionaccording to claim 16, wherein said composition is selected from anenzyme composition and a detergent composition.
 18. The compositionaccording to claim 17, wherein said detergent composition is selectedfrom a laundry detergent, a fabric softening detergent, a dishwashingdetergent, and a hard-surface cleaning product.
 19. The composition ofany one of claims 16-18, wherein said composition further comprises oneor more ions selected from calcium and/or zinc; one or more enzymestabilizer; from about 0.001% to about 1.0 weight % of said subtilisinvariant; one or more bleaching agent; one or more adjunct material;and/or one or more additional enzymes or enzyme derivatives selectedfrom the group consisting of acyl transferases, alpha-amylases,beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases,beta-galactosidases, carrageenases, catalases, cellobiohydrolases,cellulases, chondroitinases, cutinases, DNase or nuclease, endo-beta-1,4-glucanases, endo-beta-mannanases, esterases, exo-mannanases,galactanases, glucoamylases, hemicellulases, hyaluronidases,keratinases, laccases, lactases, ligninases, lipases, lipoxygenases,lysozymes, mannanases, oxidases, pectate lyases, pectin acetylesterases, pectinases, pentosanases, perhydrolases, peroxidases,phenoloxidases, phosphatases, phospholipases, phytases,polygalacturonases, proteases, pullulanases, reductases,rhamnogalacturonases, beta-glucanases, tannases, transglutaminases,xylan acetyl-esterases, xylanases, xyloglucanases, xylosidases,metalloproteases, nucleases, additional serine proteases, andcombinations thereof.
 20. The composition of any one of claims 16-19,wherein said composition contains phosphate or is phosphate-free and/orcontains boron or is boron-free.
 21. The composition of any one ofclaims 16-19, wherein said composition does not contain a proteasestabilizer.
 22. The composition of any one of claims 16-21, wherein saidcomposition is a granular, powder, solid, bar, liquid, tablet, gel,paste or unit dose composition.
 23. A method of cleaning, comprisingcontacting a surface or an item in need of cleaning with the subtilisinvariant of any one of claims 1-11 or the composition of any one ofclaims 16-21; and optionally further comprising the step of rinsing saidsurface or item after contacting said surface or item with said variantor composition, wherein, optionally, said item is dishware or fabric.24. A composition comprising the subtilisin variant of any one of claims1-11, wherein said composition is a disinfectant, industrial orinstitutional cleaning, medical instrument cleaning, contact lenscleaning, wound cleaning, or textile processing composition.
 25. Thevariant of any one of claims 1-11, wherein the variant does not have anamino acid sequence identical to a naturally occurring molecule.
 26. Thecomposition according to claim 17, wherein said enzyme composition is anenzyme granule.